Structural information of proteins are pivotal to understand their biological function. The field of structural biology is expanding and with more than 100.000 published structures in the pdb an important threshold was crossed in 2014.
Our products in this section are designed for newcomers: Pupils and students as well as scientists new to the fascinating world of protein crystallization.
The Protein Crystallization Starter Kit is designed to introduce students to the field of protein crystallization. It contains all material you need to start to grow great looking Lysozyme crystals – a real highlight in Biology or Chemistry courses!
Two different experiments can be carried out using the Protein Crystallization Starter Kit:
The kit contains two crystallization plates, cover slides and a microscope slide, a syringe pre-filled with sealing grease, all necessary buffer and salt stock solutions and a small tube containing pre-filtered Lysozyme solution.
| Products & Ordering |
| Protein Crystallization Starter Kit – English Version CS-401EN |
The JBS Crystallization Freshman Kit – Junior is addressed to newcomers in the field of protein crystallography. It is designed for screening of initial crystallization conditions of proteins, peptides, nucleic acids and macromolecular complexes in order to grow single crystals suitable for X-ray diffraction analysis.
The JBS Crystallization Freshman Kit – Junior contains the required material to crystallize your protein under investigation using the “Hanging Drop Method”:
If you are new in the field of macromolecular crystallography we recommend to read the background information before starting the experiment. The Scoring Sheet will provide help to analyse the results of your crystallization experiment.
| Products & Ordering |
| JBS Crystallization Freshman Kit – Junior CSK-101 Get a head start crystallizing your protein |
Our Crystallization Model Proteins can be utilized in crystallization experiments as well as crystallization training and demos.
We offer 2 proteins which can be easily crystallized within days as lyophilized powder or in a stabilization buffer:
| Products & Ordering |
| Lysozyme – Solution CO-401 Crystallization grade model protein |
| Proteinase K – lyophilised CO-404 Crystallization grade model protein |
The Crystal Handling Kit will help you to acquire skills in protein crystallization, crystal mounting and data collection.
Each kit contains:
| Products & Ordering |
| Crystal Handling Kit CO-150 |
Protein Crystallization is still the most challenging task on the way of protein structure determination. The best possible protein preparation before crystallization setup increases the likelihood of success dramatically. Therefore, stability prescreens (e.g. Thermofluor Screens) should be routine to search for stabilizing conditions before starting time-consuming crystallization experiments.
This section comprises crystallization screens, optimization screens, crystallization plates and accessories. It contains specific screens that are ready-to-use as well as basic screens that allow individual combination of ingredients.
| Products & Ordering |
| Frag Xtal Screen X-FS-101 Fragment Screen for Crystallographic Screening |
[1] Wollenhaupt et al. (2021) Workflow and Tools for Crystallographic Fragment Screening at the Helmholtz-Zentrum Berlin. J. Vis. Exp. 169:e62208.
[2] Huschmann et al. (2016) Structures of endothiapepsin-fragment complexes from crystallographic fragment screening using a novel, diverse and affordable 96-compound fragment library. Acta Cryst F 72:346.
[3] Schiebel et al. (2016) Six Biophysical Screening Methods Miss a Large Proportion of Crystallographic Discovered Fragment Hits: A Case Study. ACS Chem. Biol. 11:1693.
[4] Schiebel et al. (2015) One Question, Multiple Answers: Biochemical and Biophysical Screening Methods Retrieve Deviating Fragment Hit Lists. ChemMedChem 10:1511.
[5] Hajduk and Greer (2007) A decade of fragment-based drug design: strategic advances and lessons learned. Nature Reviews Drug Discovery 6:211.
[6] Rees et al. (2004) Fragment-based lead discovery. Nature Reviews Drug Discovery 3:660.
Upgraded with the Anderson−Evans polyoxotungstate [TeW6O24]6− (TEW) as universal additive, the XP Screens promote protein crystallization even for most challenging targets and improve diffraction quality of protein crystals[1]. Its potential has been shown in the new protein structures of aurone synthase from Coreopsis grandiflora[2-4] (PDB code: 4Z12, 4Z13) and mushroom tyrosinase PPO4 from Agaricus bisporus[6,7] (PDB code: 4OUA). The model protein lysozyme crystallized into a new crystal form[5] (PDB code: 4PHI).
The XP Screens are TEW-optimized JBScreen Basics: 96 of the most prominent crystallization conditions complemented with TEW as “glue” for protein molecules.
Protein-protein bridging by TEW in different orientations
Image from [1], used by courtesy of Prof. Annette Rompel, University of Vienna, Austria
[1] Bijelic et al. (2017) Ten Good Reasons for the Use of the Tellurium-Centered Anderson-Evans Polyoxotungstate in Protein Crystallography. Acc. Chem. Res. 50:1441.
[2] Molitor et al. (2016) Aurone synthase is a catechol oxidase with hydroxylase activity and provides insights into the mechanism of plant polyphenol oxidases. Proc. Natl. Acad. Sci. 113:E1806.
[3] Molitor et al. (2016) In situ formation of the first proteinogenically functionalized [TeW6O24O2(Glu)]7- structure reveals unprecedented chemical and geometrical features of the Anderson-type cluster. Chem. Commun. 52:12286.
[4] Molitor et al. (2015) Crystallization and preliminary crystallographic analysis of latent, active and recombinantly expressed aurone synthase, a polyphenol oxidase, from Coreopsis grandiflora. Acta Cryst. F 71:746.
[5] Bijelic et al. (2015) Hen Egg-White Lysozyme Crystallisation: Protein Stacking and Structure Stability Enhanced by a Tellurium(VI)-Centred Polyoxotungstate. ChemBioChem 16:233.
[6] Mauracher et al. (2014) Latent and active abPPO4 mushroom tyrosinase cocrystallized with hexatungstotellurate(VI) in a single crystal. Acta Cryst. D 70:2301.
[7] Mauracher et al. (2014) Crystallization and preliminary X-ray crystallographic analysis of latent isoform PPO4 mushroom (Agaricus bisporus) tyrosinase. Acta Cryst. F 70:263.
Access to individual screen conditions in larger volumes is important when it comes to reproducing initial hits and starting crystallization optimization, or for soaking experiments (heavy atom derivatization).
Individual conditions are available for all screens of the JBScreen Family:
Solutions are made from exactly the same chemicals as the conditions in the original screens, are sterile filtered and are available in different volumes.
Upon ordering, please indicate which condition from which screen you wish to purchase! Clicking the basket sign in the product table below will open a popup window that will allow you to enter screen name and condition number. This information will be saved in your shopping basket.
| Products & Ordering |
| Individual JBScreen Condition CS-IND Indicate screen name, Cat.# and condition # when placing the order |
JBScreen Wizard is a highly effective random sparse matrix screen for crystallizing proteins, peptides, nucleic acids and macromolecular complexes. A large range of precipitants, buffers and salts allow a broad sampling of crystallization space at pH levels from pH 4,5 to 10,5.
Bulk – 48, 96 or 192 screening solutions in 10 ml aliquots
HTS – 96 or 192 screening solutions delivered in a deep-well block, 1.7 ml per well
Preparation of JBScreen buffers
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | |
| JBScreen Wizard 1 CS-311 | JBScreen Wizard 3 & 4 CS-316 |
| JBScreen Wizard 2 CS-312 | JBScreen Wizard 1 – 4 CS-317 |
| JBScreen Wizard 3 CS-313 | JBScreen Wizard 1 & 2 HTS CS-318 |
| JBScreen Wizard 4 CS-314 | JBScreen Wizard 3 & 4 HTS CS-319 |
| JBScreen Wizard 1 & 2 CS-315 | JBScreen Wizard 1 – 4 HTS CS-320 |
The Pi-Screens were developed at the MRC Laboratory of Molecular Biology (Cambridge, UK) for efficient crystallization screening of soluble proteins (Pi-minimal Screen) and integral membrane proteins (Pi-PEG Screen). The approach is based on incomplete factorial design.
The unique formulation was generated following a strategy named Pi sampling [1] in order to create novel combinations of precipitants, buffers and additives across a standard 96-condition plate layout. Thus, the diversity amongst the crystallization conditions is ideal for initial screening.
The Pi-minimal Screen includes 36 components, i.e. 12 precipitants, 12 buffers systems and 12 salts. Buffers employed in the Pi-minimal screen are buffer systems (acid-base pairs, e.g. HEPES and HEPES sodium salt). Consequently, pH can be adjusted by mixing 2 stock solutions at different ratios during later optimizations.
The efficiency of the Pi-minimal Screen was demonstrated by the crystallization of 10 proteins before its commercialization [1].
The Pi-PEG Screen includes various polyethylene glycol mixtures, additives and buffers covering a pH range from 4,0 – 9,5 and hence is suitable for integral membrane proteins as well as for soluble proteins.
The efficiency of the Pi-PEG screen was demonstrated by the crystallization of a G-protein coupled receptor (GPCR) when quality crystals could not be produced with other commercially available screens [1].
Bulk – 4 x 24 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well
Preparation of JBScreen buffers
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | |
| Pi-minimal Screen CS-127 | Pi-minimal Screen HTS CS-211L |
| Pi-PEG Screen CS-128 | Pi-PEG Screen HTS CS-212L |
[1] Gorrec et al. (2011) Pi sampling: a methodical and flexible approach to initial macromolecular crystallization screening. Acta Cryst. D67:463.
Available online at http://journals.iucr.org/d/issues/2011/05/00/bw5391/index.html
JBScreen JCSG++ is a sparse matrix screen optimized for initial screening of crystallization conditions of biological macromolecules. The screen has been formulated by researchers from the Joint Center for Structural Genomics (JCSG) [1] and from the European Genomics Consortium [2].
96 reagents have been selected with the aim to maximize the coverage of the crystallization parameter space and to reduce the redundancy of crystallization conditions within commercially available crystallization screens. Thus, a core set of 66 conditions used by the JCSG for high-throughput structural determination [1] was extended to 96 screening conditions in order to round off the pH profile and to incorporate different precipitants such as succinate, malonate and formate.
When JBScreen JCSG++ is used along with JBScreen PACT++, the benefits of a sparse matrix screen can be combined with the systematic investigation the precipitation behaviour of the protein.
Bulk – 24 or 96 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well
Preparation of JBScreen buffers
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | |
| JBScreen JCSG++ 1 CS-151 | JBScreen JCSG++ 4 CS-154 |
| JBScreen JCSG++ 2 CS-152 | JBScreen JCSG++ 1 – 4 CS-155 |
| JBScreen JCSG++ 3 CS-153 | JBScreen JCSG++ HTS CS-206L |
[1] Page et al. (2004) Shotgun crystallization strategy for structural genomics: an optimized two-tiered crystallization screen against the Thermotoga maritima proteome. Acta Cryst. D 59:1028.
[2] Newman et al. (2005) Towards rationalization of crystallization screening for small- to medium-sized academic laboratories: the PACT/JCSG+ strategy. Acta Cryst. D 61:1426.
JBScreen PACT++ is a crystallization screen facilitating systematic pH, anion- and cation testing in the presence of polyethylene glycol (PEG) based on the work of Newman et al. [1].
The 96 unique crystallization conditions combine three mini-screens in one:
1. 24-condition PEG/pH screen
2. 24-condition PEG/cation screen
3. 48-condition PEG/anion screen
This systematic approach aims to alter individual components of the crystallization conditions, i.e. pH, anions and cations, independently from the others in order to obtain more information of the precipitation behaviour of the protein.
When JBScreen PACT++ is used along with JBScreen JCSG++, systematic investigation of the precipitation behaviour of the protein can be combined with a sparse matrix screen in order to enhance the success rate of protein crystallization.
Bulk – 24 or 96 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well
Background & Instructions on JBScreen PACT++
Preparation of JBScreen buffers
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | |
| JBScreen PACT++ 1 CS-161 | JBScreen PACT++ 2 CS-162 |
| JBScreen PACT++ 3 CS-163 | JBScreen PACT++ 4 CS-164 |
| JBScreen PACT++ HTS CS-207L | JBScreen PACT++ 1 – 4 CS-165 |
[1] Newman et al. (2005) Towards rationalization of crystallization screening for small- to medium-sized academic laboratories: the PACT/JCSG+ strategy. Acta Cryst. D 61:1426.
JBScreen Pentaerythritol has been designed for efficient crystallization screening of biological macromolecules based on pentaerythritol polymers as precipitants. The screen was developed by Ulrike Demmer from the Max-Planck-Institute for Biophysics in Frankfurt.
The choice of a suitable precipitant is of crucial importance for the crystallization of proteins. JBScreen Pentaerythritol utilizes two novel precipitating agents, i.e. pentaerythritol propoxylate and pentaerythritol ethoxylate. Both are branched polymers containing a pentaerythritol backbone. Thus they differ from more traditional precipitants like MPD and PEG’s in size and nature.
In addition, pentaerythritol polymers function as cryoprotectants. Protein crystals grown in high concentrations of these precipitants can be frozen directly from the crystallization drop. The successful application of pentaerythritol polymers to yield protein crystals was first described by Gulick et al. [1]. Furthermore, this class of precipitants has been used for membrane crystallization: The X-ray structure of cbb3 Cytochrome Oxidase was published in Science in 2010. Crystals of this proton pumping membrane protein were successfully grown using pentaerythritol ethoxylate as precipitation agent [2].
JBScreen Pentaerythritol comprises of 96 unique conditions, based on 4 different pentaerythritol polymers as precipitating agent:
The 4 polymers are arranged to a grid screen, thus allowing screening i) of three different precipitant concentrations, ii) four different pH values and iii) with and without the addition of salts, i.e. magnesium chloride, ammonium sulfate, potassium chloride.
The advantage of JBScreen Pentaerythritol not only lies in the novel 96 conditions but also in the systematic arrangement of the unique reagents, which enables the user to compare individual conditions directly. Even if initial screening may not always yield crystals, valuable information about the protein under investigation can be obtained from the scoring sheet.
Bulk – 24 or 96 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well
JBScreen Pentaerythritol Scoring Sheet
Preparation of JBScreen buffers
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | |
| JBScreen Pentaerythritol 1 CS-191 (PEP 426 based) | JBScreen Pentaerythritol 2 CS-192 (PEP 629 based) |
| JBScreen Pentaerythritol 3 CS-193 (PEE 270 based) | JBScreen Pentaerythritol 4 CS-194 (PEE 797 based) |
| JBScreen Pentaerythritol 1 – 4 CS-195 | JBScreen Pentaerythritol HTS CS-210L |
[1] Gulick et al. (2002) Pentaerythritol propoxylate: a new crystallization agent and cryoprotectant induces crystal growth of 2-methylcitrate dehydratase. Acta Cryst. D58:306.
[2] Buschmann et al. (2010) The Structure of cbb3 Cytochrome Oxidase Provides Insights into Proton Pumping. Science 329:327.
JBScreen PEG/Salt is an effective reagent kit designed for initial screening of crystallization conditions of biological macromolecules.
It comprises high-purity PEG 3350 and PEG 5000 MME, each combined with 48 different salts, thus covering a range of anions and cations most frequently used in bio-crystallography. The unique combination of the reagents allows screening of PEG versus ionic strength, ion type and pH.
Bulk – 24 or 96 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well
Preparation of JBScreen buffers
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | |
| JBScreen PEG/Salt 1 CS-141 | JBScreen PEG/Salt 2 CS-142 |
| JBScreen PEG/Salt 3 CS-143 | JBScreen PEG/Salt 4 CS-144 |
| JBScreen PEG/Salt 1 – 4 CS-145 | JBScreen PEG/Salt HTS CS-205L |
JBScreen Nuc-Pro is designed to screen for preliminary crystallization conditions of nucleic acids and protein-nucleic acid complexes.
The highly effective sparse matrix screen is based upon extensive screening of the PDB, with focus on entries by structural genomic initiatives, the BMCD and other protocols [1-3]. Reported crystallization conditions for various RNAs, DNAs as well as protein-nucleic acid complexes were compiled and analyzed for rate of recurrence.
The 96 conditions selected cover a variety of polymers, mono- and divalent metal ions, organics, alcohols and buffers of a pH range from 4,0 to 8,5. The organization of the reagents into individual kits is based upon the main precipitant, i.e. various molecular weight PEGs, Salts, alcohols (MPD and 2-Propanol).
Bulk – 24 or 96 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well
The ready-to-use reagents are tested for DNase contamination using our DNase Detection Kit → Molecular Biology.
Preparation of JBScreen buffers
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | |
| JBScreen Nuc-Pro 1 CS-181 | JBScreen Nuc-Pro 2 CS-182 |
| JBScreen Nuc-Pro 3 CS-183 | JBScreen Nuc-Pro 4 CS-184 |
| JBScreen Nuc-Pro 1 – 4 CS-185 | JBScreen Nuc-Pro HTS CS-209L |
[1] Doudna et al. (1993) Crystallization of ribozymes and small RNA motifs by a sparse matrix approach. Proc. Natl. Sci. USA 90:7829.
[2] Scott et al. (1995) Rapid Crystallization of Chemically Synthesized Hammerhead RNAs using a Double Screening Procedure. J. Mol. Biol. 250:327.
[3] Ke et al. (2004) Crystallization of RNA and RNA-protein complexes. Methods 34:408.
JBScreen Kinase is a highly specialized screen formulated for the determination of initial crystallization conditions of protein kinases.
Through the use of advanced data mining, crystallization conditions of kinases have been identified from published structures. Data evaluation and verification resulted in the formulation of 96 unique reagents, highly effective for the crystallization of kinases.
JBScreen Kinase utilizes a variety of different precipitating agents, i.e. various molecular weight PEGs, MPD and Ammonium Sulfate, in combination with buffers covering a pH range from 3,1 – 10,0 and numerous additives.
Bulk – 24 or 96 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well
Preparation of JBScreen buffers
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | |
| JBScreen Kinase 1 CS-131 | JBScreen Kinase 2 CS-132 |
| JBScreen Kinase 3 CS-133 | JBScreen Kinase 4 CS-134 |
| JBScreen Kinase 1 – 4 CS-135 | JBScreen Kinase HTS CS-204L |
JBScreen Membrane covers 96 of the most successful conditions for crystallization of membrane proteins. Each individual composition results from an extensive analysis of the crystallization conditions that have yielded membrane protein structures so far.
The JBScreen Membrane crystallization conditions are primarily ordered by type and concentration of the precipitant. This allows easy extraction of all relevant information for a straightforward refinement: Once you get a hit, you immediately see the effects of the neighbouring conditions. The subsequent fine tuning of preliminary hits will be much more efficient.
JBScreen Detergents perfectly complement JBScreen Membrane: This combination enables you to screen a broad range of detergents, while concentrating on the most successful crystallization conditions, making crystallization screening of membrane proteins much more efficient and less time consuming.
Bulk – 24 or 96 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well
Preparation of JBScreen buffers
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | |
| JBScreen Membrane 1 CS-301L (PEG 400 to PEG 2000 MME based) | JBScreen Membrane 2 CS-302L (PEG 2000 MME to PEG 10000 based) |
| JBScreen Membrane 3 CS-303L (Ammonium Sulfate, Alcohol and Salt based) | JBScreen Membrane 4 CS-304L (MPD, Salt based) |
| JBScreen Membrane 1 – 4 CS-309 | JBScreen Membrane HTS CS-310 |
| JBScreen Membrane 1 – 4 & JBScreen Detergents HTS CS-308 |
JBScreen LCP is a crystallization screen designed for efficient screening of crystallization conditions in the Lipidic Cubic Phase (LCP), which has become the method of choice for membrane protein crystallization in different types of LCP lipids.
The 96 conditions of JBScreen LCP result from data mining of 192 integral membrane proteins, that were successfully crystallized by the in meso method and have yielded structures [1].
The screen is ordered by type and concentration of the precipitant and is free of cacodylate.
Cartoon representation of the events proposed to take place during the crystallization of an integral membrane protein from the lipid cubic mesophase. Image from [1], used by courtesy of Prof. Martin Caffrey, Trinity College Dublin, Ireland.
Bulk – 4 x 24 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well
Preparation of JBScreen buffers
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | |
| JBScreen LCP CS-340 | JBScreen LCP HTS CS-213L |
[1] Caffrey (2015) A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and soluble proteins and complexes. Acta Cryst F 71:3.
Despite intensive research, the crystallization of biological macromolecules remains a process of trial and error. Nucleation and crystal growth are influenced by the interaction of many variables, such as temperature, pH, precipitant and salt concentration.
Testing all possible combinations would be too time consuming and would require enormous amounts of sample. One approach to find suitable crystallization conditions is the sparse-matrix method. This method involves screening with an intentional bias towards conditions which have been proven successful in the crystallization of biological macromolecules.
In 1991, Jancarik and Kim published 50 conditions, which were derived from previously crystallized proteins [1]. These and other conditions form the basis of the JBScreen Basic system [1,2]. However, JBScreen Basic is designed to fit the 24-well plate format and like in all other JBScreen crystallization kits, we abstained from the use of cacodylate buffers and replaced them with MES. JBScreen Basic contains 96 unique reagent mixtures for screening a wide range of pH and various salts and precipitants.
Bulk – 24 or 96 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well
Preparation of JBScreen buffers
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | ||
| JBScreen Basic 1 CS-121 | JBScreen Basic 2 CS-122 | JBScreen Basic 3 CS-123 |
| JBScreen Basic 4 CS-124 | JBScreen Basic 1 – 4 CS-125 | JBScreen Basic HTS CS-203L |
[1] Jancarik and Kim (1991) Sparse matrix sampling: a screening method for crystallization of proteins. J. Appl. Cryst. 24:409.
[2] Cudney et al. (1994) Screening and optimization strategies for macromolecular crystal growth. Acta Cryst. D 50:414.
JBScreen Classic is a crystallization kit designed for efficient and flexible screening of crystallization conditions for proteins, peptides, nucleic acids, macromolecular complexes and water-soluble small molecules.
The JBScreen Classic Kits 1-10 cover 240 of the most prominent buffers for protein crystallization. Their compositions result from data mining of several thousands of crystallized proteins. JBScreen Classic represents the statistically most successful buffers that yielded protein crystals suitable for X-ray diffraction.
The JBScreen Classic buffers are principally ordered by type and concentration of the precipitant. This allows easy extraction of all relevant information and is already a first step to a refinement: Once you get a hit, you immediately see the effects of the neighbouring conditions. Subsequent fine tuning of preliminary hits will be much more efficient.
JBScreen Classic comprises 10 kits of 24 unique reagents in the standard 10 ml bulk format.
JBScreen Classic HTS I+II contains the formulations of the JBScreen system, adopted to fit the 96-well format for high throughput crystallization applications. Each JBScreen Classic HTS deep-well block is pre-filled with 96 sterile conditions at 1.7 ml each.
Preparation of JBScreen buffers
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | ||
| JBScreen Classic 1 CS-101L (PEG 400 to 3000 based) | JBScreen Classic 2 CS-102L (PEG 4000 based) | JBScreen Classic 3 CS-103L (PEG 4000+ based) |
| JBScreen Classic 4 CS-104L (PEG 5000 MME to 8000 based) | JBScreen Classic 5 CS-105L (PEG 8000 to 20000 based) | JBScreen Classic 6 CS-106L (Ammonium Sulfate based) |
| JBScreen Classic 7 CS-107L (MPD based) | JBScreen Classic 8 CS-108L (MPD/Alcohol based) | JBScreen Classic 9 CS-109L (Alcohol/Salt based) |
| JBScreen Classic 10 CS-110L (Salt based) | JBScreen Classic 1 – 5 CS-112L | JBScreen Classic 6 – 10 CS-113L |
| JBScreen Classic 1 – 10 CS-114L | JBScreen Classic HTS I CS-201L (PEG based) | JBScreen Classic HTS II CS-202L (Ammonium Sulfate, MPD, Alcohol and Salt based) |
The Thermofluor Screens JBScreen FUNDAMENT and JBScreen SPECIFIC allow identification of protein-stabilizing buffer conditions which is pivotal for protein purification, characterization and crystallization.
Undesired overlay of screening of interdependent variables is prevented by strictly categorizing stability screening of proteins into
1. FUNDAMENTAL factors that influence the whole protein molecule (pH and ionic strength)
2. SPECIFIC factors that affect energetically important hot spots on the protein (substrates and their analogs, cations, anions, …)
The protein’s melting temperature (Tm) is used as reporter for protein stability and determined by a thermal shift assay (96-well plate format) monitoring the unfolding of a protein in a temperature-dependent manner. The higher the Tm, the higher is the thermostability of the protein in that specific environment.
JBScreen Thermofluor FUNDAMENT and SPECIFIC are provided in a deep-well block at 0.5 ml each, which allows a flexible application of this alternative approach.
α-Chymotrypsinogen A was applied in JBScreen Thermofluor FUNDAMENT and SPECIFIC.
Stabilizing conditions (high ionic strength, neutral pH, CaCl2 & FeCl3) were combined without further optimization. A crystallization screen was set up:
Talk held at HEC19 in Warberg, September 29th, 2016
JBScreen Detergents contain 4 x 24 unique detergents that are compatible with most common crystallization reagents and are therefore perfectly suited for membrane protein solubilization:
JBScreen Detergents can be used throughout the protein purification process or can be added afterwards by dialysis or ion-exchange chromatography (detergent exchange). Detergent exchange can be vital for obtaining well-diffracting membrane-protein crystals [1].
JBScreen Detergents is also valuable for additive screening with detergents and detergent mixtures [2,3] in combination with the JBScreen Membrane. This combination will enable you to screen a broad range of detergents, while concentrating on the most successful crystallization conditions, making crystallization screening of membrane proteins much more efficient and less time consuming.
Screen for stabilizing detergents by combining JBScreen Detergents with Prometheus NT.48, a label-free nanoDSF technology developed by NanoTemper Technologies, ideally suited for membrane protein stabilization.
[1] Rosenow et al. (2003) The influence of detergents and amphiphiles on the solubility of the light harvesting complex. Acta Cryst. D59:1422
[2] Adir (1999) Crystallization of the oxygen-evolving reaction centre of photosystem II in nine different detergent mixtures. Acta Cryst. D55:891
[3] Koronakis et al. (2000) Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405:914
JBScreen Plus is an additive screen most useful in the optimization of preliminary crystallization conditions. The selection of the additives is based on the Hofmeister series, which reflects the ability of ions to stabilize the structure of proteins. Thus ions can be classified as either kosmotropic or chaotropic. The first having structure stabilizing properties, thus they may assist in, e.g. crystallizing proteins with a high proportion of flexible loop regions. The latter show structure disturbing properties which may assist in the crystallization of large complexes allowing them to re-arrange to form favorable crystal contacts.
JBScreen Plus consists of 5 individual kits, JBScreen Plus Kosmotropic, JBScreen Plus Chaotropic, JBScreen Plus Salts, JBScreen Plus Additives and JBScreen Plus Volatiles, containing 24 different additives each. The ready-to-use reagents are supplied in 1 ml aliquots.
The 96 solutions of JBScreen Plus HTS, comprising the reagents of the kosmotropic, chaotropic, salts and additive kit, are supplied in a sterile deep well block containing 1 ml per well.
| Products & Ordering | |
| JBScreen Detergents 1 CS-521 | JBScreen Detergents 4 CS-524 |
| JBScreen Detergents 2 CS-522 | JBScreen Detergents HTS CS-525 |
| JBScreen Detergents 3 CS-523 | JBScreen Membrane 1 – 4 & JBScreen Detergents HTS CS-308 |
Common buffers at 0.5 M concentration provided in a deep well block (1.7 ml of each condition).
Choose between JBScreen Buffers (neutral pH range from 5.5 – 8.5) and JBScreen Buffers Xtreme (extreme pH ranges from 3.0 – 5.5 and 8.5 – 11.0).
Suitable as follow-up screens for JBScreen Thermofluor or as standard buffer screens.
Since there is no such thing as a standard buffer for all proteins, success of purification and downstream processing of a particular protein of interest greatly depends on identification of a buffer environment that facilitates the protein’s stability & homogeneity in solution. Thus, in most labs it has become routine to search for stabilizing conditions before starting time-consuming crystallization experiments. Choose your favorite from a number of screens.
JBScreen Solubility HTS, developed by Meindert Lamers from the MRC in Cambridge, is designed to quickly find suitable buffer components to purify and store protein in.
JBScreen Solubility HTS tests for buffer, pH, salt and glycerol at the same time: For all proteins investigated, suitable conditions were found in a single assay. Protein and buffer conditions are dispensed in a ratio of 1:3, thereby minimizing the effect of any buffer components in which the protein is initially stored. Standard crystallization robots set up the assay in 5 minutes and very small amounts of protein are required (10 µl @ 5-10 mg/ml). The results are visible after one hour at high protein concentration or 12 hours at low protein concentration:
Examples of a drop without protein precipitation (left) and a drop with protein precipitation (right)
Manual JBScreen Solubility HTS
| Products & Ordering |
| JBScreen Solubility HTS CO-311 |
The JBS Solubility Kit is a pre-crystallization screen to improve the composition of the initial protein buffer solution prior to performing crystallization set-ups [1]. Since the highly complex properties of proteins are dependent on their environment, buffer solutions play an important role, i.e. influencing the solubility and the aggregation behaviour of the protein sample.
Studies have shown that aggregation of the protein may inhibit nucleation and crystal growth. Therefore, the JBS Solubility Kit has been developed to investigate protein samples towards their homogeneity and monodispersity prior to crystallization trials, employing hanging drop vapour diffusion experiments combined with dynamic light scattering.
The JBS Solubility Kit contains a set of 24 buffer solutions at different pH-values for setting up hanging drop vapour diffusion experiments in order to monitor the aggregation and precipitation of the protein sample, and a set of 14 additives used for further optimization employing dynamic light scattering.
| Products & Ordering |
| JBS Solubility Kit CO-310 |
[1] Jancarik et al. (2004) Optimum solubility (OS) screening: an efficient method to optimize buffer conditions for homogeneity and crystallization of proteins. Acta Cryst D 60:1670.
The Thermofluor Screens JBScreen FUNDAMENT and JBScreen SPECIFIC allow identification of protein-stabilizing buffer conditions which is pivotal for protein purification, characterization and crystallization.
Undesired overlay of screening of interdependent variables is prevented by strictly categorizing stability screening of proteins into
1. FUNDAMENTAL factors that influence the whole protein molecule (pH and ionic strength)
2. SPECIFIC factors that affect energetically important hot spots on the protein (substrates and their analogs, cations, anions, …)
The protein’s melting temperature (Tm) is used as reporter for protein stability and determined by a thermal shift assay (96-well plate format) monitoring the unfolding of a protein in a temperature-dependent manner. The higher the Tm, the higher is the thermostability of the protein in that specific environment.
JBScreen Thermofluor FUNDAMENT and SPECIFIC are provided in a deep-well block at 0.5 ml each, which allows a flexible application of this alternative approach.
α-Chymotrypsinogen A was applied in JBScreen Thermofluor FUNDAMENT and SPECIFIC.
Stabilizing conditions (high ionic strength, neutral pH, CaCl2 & FeCl3) were combined without further optimization. A crystallization screen was set up:
Crystal growth was promoted by the stabilizing specific ions CaCl2 & FeCl3 from JBScreen Thermofluor SPECIFIC.
Talk held at HEC19 in Warberg, September 29th, 2016
| Products & Ordering | ||
| JBScreen Thermofluor FUNDAMENT CS-332 Thermal Shift Assay for protein stability | JBScreen Thermofluor SPECIFIC CS-333 Thermal Shift Assay for protein stability | JBS Thermofluor Dye X-TD |
Monoclonal antibodies are important tools for treating numerous diseases such as cancer, autoimmune, and inflammatory conditions. As of 2018, over 80 monoclonal antibody drugs have been approved for clinical use by the FDA (Food and Drug Administration, USA) and the EMA (European Medicines Agency, EU). Key steps in the development of therapeutic antibodies are the optimization of their short- and long-term stability, as well as preformulation and final formulation conditions.
The FORMOscreen® is an antibody formulation screen compatible with biophysical and biochemical read-out (e.g. DSF, nanoDSF, DSC, DLS, SLS, LC-MS, HPLC-SEC, ELISA,…) allowing for quick and easy analysis of important antibody parameters: Chemical, thermal, colloidal, and conformational stability, long-term storage stability, forced-degradation resistance, as well as biochemical activity and antigen-binding.
The FORMOscreen® conditions, derived from the formulations of therapeutic antibodies approved by the FDA and EMA, have already shown to have positive effects on antibody formulation and stability and thus provide optimal starting points for developing preformulations for therapeutic and diagnostic antibody candidates.
2bind Application Note: FORMOscreen® – Formulations of Developed Antibodies
| Products & Ordering |
| FORMOscreen® CS-360 Antibody Formulation Screen |
This section comprises crystal dyes to discriminate between macromolecular crystals and salt crystals as well as suitable oils for microbatch crystallization experiments.
How can you be sure that your precious crystals are protein and not salt?
With the help of JBS Crystal Dyes you can discriminate between macromolecular crystals and salt crystals within minutes. Whatever suits your taste, you can stain your crystals blue, purple, green or red. All our crystal dyes are small molecules which are able to permeate the solvent channels of proteins and thus, staining them. In contrast, salt crystals will remain colorless.
Our JBS Black Light is a nonspecific fluorescent crystal dye used for the detection of protein crystals in crystallization trials. The fluorescence signal can be exploited to contrast protein crystals above background artifacts and enables the detection of microcrystals, even if they are located under a protein skin. Thus, the dye is suitable for automatic crystal detection.
| Products & Ordering | |
| JBS True Blue CO-301 | JBS Bright Red CO-304 |
| JBS Deep Purple CO-302 | JBS Rainbow CO-305 Set of JBS Deep Purple, JBS True Blue, JBS Xtal Green and JBS Bright Red |
| JBS Xtal Green CO-303 | JBS Black Light CO-306 Fluorescent Crystal Dye |
Silicone oil for Under Oil Crystallization Plates.
Adequate for 10 Plates.
| Products & Ordering |
| Silicone Oil CO-201 |
Membrane proteins play a key role to understand the complex interactions that allow for unicellular and multicellular life up to humans. They further possess a huge potential for the treatment of human diseases and structure determination is the first bottleneck on this promising and challenging way.
This section comprises specialized screens and tools to crystallize membrane proteins solubilized by detergents as well as membrane proteins in the lipidic cubic phase (LCP). Amphipol A8-35 is a surfactant especially useful for sample preparation in Cryo-EM – to stabilize membrane proteins in a detergent-free aqueous solution.
JBScreen LCP is a crystallization screen designed for efficient screening of crystallization conditions in the Lipidic Cubic Phase (LCP), which has become the method of choice for membrane protein crystallization in different types of LCP lipids.
The 96 conditions of JBScreen LCP result from data mining of 192 integral membrane proteins, that were successfully crystallized by the in meso method and have yielded structures [1].
The screen is ordered by type and concentration of the precipitant and is free of cacodylate.
Cartoon representation of the events proposed to take place during the crystallization of an integral membrane protein from the lipid cubic mesophase. Image from [1], used by courtesy of Prof. Martin Caffrey, Trinity College Dublin, Ireland.
[1] Caffrey (2015) A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and soluble proteins and complexes. Acta Cryst F 71:3.
JBScreen Membrane covers 96 of the most successful conditions for crystallization of membrane proteins. Each individual composition results from an extensive analysis of the crystallization conditions that have yielded membrane protein structures so far.
The JBScreen Membrane crystallization conditions are primarily ordered by type and concentration of the precipitant. This allows easy extraction of all relevant information for a straightforward refinement: Once you get a hit, you immediately see the effects of the neighbouring conditions. The subsequent fine tuning of preliminary hits will be much more efficient.
JBScreen Detergents perfectly complement JBScreen Membrane: This combination enables you to screen a broad range of detergents, while concentrating on the most successful crystallization conditions, making crystallization screening of membrane proteins much more efficient and less time consuming.
Bulk – 24 or 96 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
Bulk – 24 or 96 screening solutions in 10 ml aliquots
HTS – 96 screening solutions delivered in a deep-well block, 1.7 ml per well
Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.
| Products & Ordering | |
| JBScreen Membrane 1 CS-301L (PEG 400 to PEG 2000 MME based) | JBScreen Membrane 1 – 4 CS-309 |
| JBScreen Membrane 2 CS-302L (PEG 2000 MME to PEG 10000 based) | JBScreen Membrane HTS CS-310 |
| JBScreen Membrane 3 CS-303L (Ammonium Sulfate, Alcohol and Salt based) | JBScreen Membrane 1 – 4 & JBScreen Detergents HTS CS-308 |
| JBScreen Membrane 4 CS-304L |
JBScreen Detergents contain 4 x 24 unique detergents that are compatible with most common crystallization reagents and are therefore perfectly suited for membrane protein solubilization:
JBScreen Detergents can be used throughout the protein purification process or can be added afterwards by dialysis or ion-exchange chromatography (detergent exchange). Detergent exchange can be vital for obtaining well-diffracting membrane-protein crystals [1].
JBScreen Detergents is also valuable for additive screening with detergents and detergent mixtures [2,3] in combination with the JBScreen Membrane. This combination will enable you to screen a broad range of detergents, while concentrating on the most successful crystallization conditions, making crystallization screening of membrane proteins much more efficient and less time consuming.
Screen for stabilizing detergents by combining JBScreen Detergents with Prometheus NT.48, a label-free nanoDSF technology developed by NanoTemper Technologies, ideally suited for membrane protein stabilization.
[1] Rosenow et al. (2003) The influence of detergents and amphiphiles on the solubility of the light harvesting complex. Acta Cryst. D59:1422
[2] Adir (1999) Crystallization of the oxygen-evolving reaction centre of photosystem II in nine different detergent mixtures. Acta Cryst. D55:891
[3] Koronakis et al. (2000) Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405:914
Amphipols are short amphipatic polymers that are specifically designed to stabilize membrane proteins in aqueous solutions.
Due to their dense distribution of hydrophobic chains they tightly bind to transmembrane surfaces of membrane proteins and cover it with a thin interfacial layer of surfactant[1]. The resulting small hydrophilic complexes have several advantages over usually much larger protein detergent complexes, such as stability and functionality of the membrane protein.
Amphipol A8-35 is successfully applied as stabilizing agent in Cryo-EM[2-5] and X-ray crystallography[6].
| Products & Ordering |
| Amphipol A8-35 X-A835 |
[1] Zoonens et al. (2014) Amphipols for Each Season. J Membrane Biol 247:759.
[2] Chen et al. (2016) Structure of the STRA6 receptor for retinol uptake. Science 353:887.
[3] Zubcevic et al. (2016) Cryo-Electron Microscopy of the Trpv2 Ion Channel. Nat Struct Mol Biol 23:180.
[4] Bai et al. (2015) Sampling the conformational space of the catalytic subunit of human gamma-secretase. DOI 10.7554/eLife.11182.
[5] Althoff et al. (2011) Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1. EMBO J 30:4652.
[6] Polovinkin et al. (2014) High-Resolution Structure of a Membrane Protein Transferred from Amphipol to a Lipidic Mesophase. J Membrane Biol 247:997.
Membrane protein crystallization using lipidic cubic phase (LCP) is proving to be a successful methodology for obtaining good quality diffracting crystals from membrane proteins due to its membrane native-like environment[1].
Monoolein is the first choice lipid for performing an LCP crystallization experiment. However, since the nature of the lipid determines the nature of the LCP, it’s worth varying the LCP characteristics by screening different lipids, especially when initial crystallization attempts with monoolein have failed[2,3].
The anionic phospholipid DSPG is used in combination with monoacylglycerols (MAGs) to create thermodynamically stable ultraswollen bicontinuous cubic phases with water channels five times larger than traditional lipidic mesophases, suitable for the crystallization of membrane proteins with large extracellular domains[4].
The LCP host lipids & phospholipids listed below are suited to form a stable lipidic cubic phase for membrane protein crystallization.
| Products & Ordering | |
| Monoolein X-LCP-101 9.9 MAG | Monopalmitolein X-LCP-102 9.7 MAG |
| Monovaccenin X-LCP-103 11.7 MAG | Monoeicosenoin X-LCP-104 11.9 MAG |
| 7.7 MAG X-LCP-105 1-(7Z-tetradecenoyl)-rac-glycerol | 7.8 MAG X-LCP-106 1-(7Z-pentadecenoyl)-rac-glycerol |
| 7.9 MAG X-LCP-107 1-(7Z-hexadecenoyl)-rac-glycerol | DSPG X-LCP-108 1,2-Distearoyl-sn-glycero-3-phospho-rac-glycerol, sodium salt |
[1] Landau and Rosenbusch (1996) Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. PNAS 93:14532.
[2] Caffrey (2015) A comprehensive review of the lipid cubic phase or in meso method for crystallizing membrane and soluble proteins and complexes. Acta Cryst F 71:3.
[3] Caffrey and Cherezov (2009) Crystallizing Membrane Proteins Using Lipidic Mesophases. Nat Protoc. 4(5):706.
[4] Zabara et al. (2018) Design of ultra-swollen lipidic mesophases for the crystallization of membrane proteins with large extracellular domains. Nat. Commun. 9:544.
The LCP Mixer Kit is designed for manual preparation of the Lipidic Cubic Phase (LCP). It is developed by Douglas Instruments (UK) and has several advantages over other LCP Mixer Kits and Sets:
| Products & Ordering |
| LCP Mixer Kit X-LCP-M contains Mixer rail and 2 Hamilton syringes |
LCP crystallization is the most popular method for membrane protein structure determination. Experiments are typically done in batch format. However, it is well known from the crystallization of soluble proteins that vapor diffusion can be a lot more powerful. The controlled in meso phase (CIMP) method combines the benefits of LCP and vapor diffusion to push membrane protein crystallization to new limits [1]. The patent-pending In-Meso Crystallization Plate provides an easy start with this revolutionary method.
Relationship between dilution of precipitant solution in the protein well, water content of the equilibrated protein drop, and the in meso phase that can be reached in a given experiment. Adapted from [1].
| Products & Ordering |
[1] Kubicek et al. (2012) Controlled In Meso Phase Crystallization – A Method for the Structural Investigation of Membrane Proteins. PLoS ONE 7:e35458.
The new IMISX Plate, complying with the SBS standard, is an exciting development for LCP crystallization.
The IMISX™ Plate is designed to perform in meso in situ serial X-ray crystallography of soluble and membrane proteins [1].
The 96-well dual-sandwich IMISX™ Plate can be easily setup by hand or with an LCP dispensing robot. An SBS standard 96-well microplate footprint makes this plate compatible with standard robots and imagers.
By combining the standard LCP crystallization plate format with an advanced X-ray transparent thin-film design, the IMISX™ Plate allows for crystal growth and X-ray diffraction data collection like never before.
The thin-film sandwich design used for crystallization can be easily removed in sections and mounted onto an adaptor for use on standard goniometers for in situ X-ray diffraction data collection.
The IMISX™ Plate Goniometer Adaptor is part of the IMISX™ Plate Kit.
| Products & Ordering |
[1] Huang et al. (2015) In meso in situ serial X-ray crystallography of soluble and membrane proteins. Acta Cryst D 71:1238.
The LCP Glass Sandwich Set is perfectly suited for in meso crystallization of membrane proteins.
It consists of a base glass plate with an adhered double sticky spacer containing 96 wells, protected by a brown cover sheet. The glass cover slip easily seals the entire base plate.
The LCP Glass Sandwich Set was developed at the Scripps Research Institute, La Jolla, CA and is manufactured by Paul Marienfeld GmbH, Germany.
| Products & Ordering |
|
LCP Glass Sandwich Set CPL-159
|
The Lipidic Cubic Phase Crystallizations (LCP) kit facilitates the automation and increased throughput of LCP crystallization set-ups. This novel system enables LCP screening to be performed accurately and with ease – using manual – or automated systems to complete the delivery of the solutions.
Box of 20 plates
The product comprises a base plate with low tack 700 micron thickness slide and top sealing tape of 100 microns – a brown ready to remove cover sheet and separate 200 micron UVP cover film with protective dust cover. The kit is completed with a SWISSCI plate leveling device.
| Products & Ordering |
|
Lipidic Cubic Phase screening kit CPL-156
|
Kits and screens to increase protein solubility and stability prior to crystallization as well as screens to optimize the chemical composition of your crystallization reagents, i.e. buffer pH, precipitant and additive composition.
Get your protein ready for crystallization! Consider to alter the protein surface or modify the sequence by truncation or mutagenesis. Or try a new mode of production.
Do not discard bad diffracting crystals! They can be very useful, too. Try to improve diffraction by varying the solvent content or use your initial crystals for seeding.
Crystallization stock solutions, i.e. polymers, buffers and salts are ideal for the optimization of your crystallization conditions.
Using the same chemicals as utilized in the JBScreens ensures higher reproducibility of your experiments. Crystallization Stock Solutions are ready for use: the concentration is adjusted and most of them are sterile filtered.
| Products & Ordering | ||
| Pentaerythritol ethoxylate (15/4 EO/OH) – 60 % w/v CSS-374 PEE 797 | Pentaerythritol ethoxylate (15/4 EO/OH) – 100 % v/v CSS-375 PEE 797 | Pentaerythritol propoxylate (17/8 PO/OH) – 60 % w/v CSS-376 PEP 629 |
| Pentaerythritol propoxylate (17/8 PO/OH) – 100 % v/v CSS-377 PEP 629 | Pentaerythritol propoxylate (5/4 PO/OH) – 60 % w/v CSS-378 PEP 426 | Pentaerythritol propoxylate (5/4 PO/OH) – 100 % v/v CSS-379 PEP 426 |
| Polyethyleneglycol 200 – 100 % v/v CSS-396 PEG 200 | Polyethyleneglycol 300 – 100 % v/v CSS-397 PEG 300 | Polyethyleneglycol 350 Monomethylether – 50 % v/v CSS-381 PEG 350 MME |
| Polyethyleneglycol 400 – 100 % v/v CSS-252 PEG 400 | Polyethyleneglycol 550 Monomethylether – 50 % v/v CSS-236 PEG 550 MME | Polyethyleneglycol 550 Monomethylether – 50 % w/v CSS-237 PEG 550 MME |
| Polyethyleneglycol 600 – 50 % v/v CSS-241 PEG 600 | Polyethyleneglycol 600 – 50 % w/v CSS-240 PEG 600 | Polyethyleneglycol 1000 – 50 % w/v CSS-242 PEG 1000 |
| Polyethyleneglycol 1500 – 50 % w/v CSS-244 PEG 1500 | Polyethyleneglycol 2000 – 50 % w/v CSS-245 PEG 2000 | Polyethyleneglycol 2000 Monomethylether – 50 % w/v CSS-234 PEG 2000 MME |
| Polyethyleneglycol 3000 – 50 % w/v CSS-248 PEG 3000 | Polyethyleneglycol 3350 – 50 % w/v CSS-249 PEG 3350 | Polyethyleneglycol 4000 – 50 % w/v CSS-253 PEG 4000 |
| Polyethyleneglycol 5000 Monomethylether – 50 % w/v CSS-235 PEG 5000 MME | Polyethyleneglycol 6000 – 50 % w/v CSS-255 PEG 6000 | Polyethyleneglycol 8000 – 50 % w/v CSS-256 PEG 8000 |
| Polyethyleneglycol 10000 – 50 % w/v CSS-243 PEG 10000 | Polyethyleneglycol 20000 – 50 % w/v CSS-246 PEG 20000 | Polyethylenimine – 50 % w/v CSS-257 |
| Jeffamine M-600 – 50 % v/v – pH 7.0 CSS-196 | Jeffamine ED-2001 – 50 % w/v pH 7.0 CSS-406 | Poly(acrylic acid sodium salt) – 50 % w/v CSS-422 sterile filtered |
Crystallization stock solutions, i.e. polymers, buffers and salts are ideal for the optimization of your crystallization conditions.
Using the same chemicals as utilized in the JBScreens ensures higher reproducibility of your experiments. Crystallization Stock Solutions are ready for use: the concentration is adjusted and most of them are sterile filtered.
| Products & Ordering | ||
| 1,3-Propanediol – 50 % v/v CSS-104 | MPD – 100 % v/v CSS-117 (+/-)-2-Methyl-2,4-Pentanediol | Propylene Glycol – 50 % v/v CSS-280 1,2-Propanediol |
| 1,4-Dioxane – 50 % v/v CSS-107 | Ethanol – 50 % v/v CSS-330 | tert-Butanol – 50 % v/v CSS-311 |
| 1,4-Dioxane – 50 % w/v CSS-106 | Ethylene glycol – 100 % v/v CSS-183 | tert-Butanol – 50 % w/v CSS-310 |
| 1,6-Hexanediol – 5 M CSS-109 | Glycerol – 100 % v/v CSS-188 Glycerin | Triethyleneglycol – 50 % w/v CSS-314 |
| 2,5-Hexanediol – 8 % v/v CSS-419 | L-Glutathion reduced – 0.16 M CSS-199 sterile filtered | |
| 1,4-Butanediol – 50 % v/v CSS-386 | Methanol – 50 % w/v CSS-224 |
Crystallization stock solutions, i.e. polymers, buffers and salts are ideal for the optimization of your crystallization conditions.
Using the same chemicals as utilized in the JBScreens ensures higher reproducibility of your experiments. Crystallization Stock Solutions are ready for use: the concentration is adjusted and they are sterile filtered.
| Products & Ordering | ||
| ADA – 1 M CSS-501 any pH value, useful buffer range: pH 6.0 – 7.2 sterile filtered | Ammonium Acetate – 1 M CSS-527 any pH value, useful buffer range: pH 3.6 – 5.6 sterile filtered | AMPD – 1 M CSS-528 any pH value, useful buffer range: pH 7.8 – 9.7 sterile filtered |
| Bicine – 1 M CSS-502 any pH value, useful buffer range: pH 7.6 – 9.5 sterile filtered | BIS-TRIS – 1 M CSS-503 any pH value, useful buffer range: pH 5.8 – 7.2 sterile filtered | BIS-TRIS Propane – 1 M CSS-504 any pH value, useful buffer range: pH 6.3 – 9.5 sterile filtered |
| CAPS – 1 M CSS-505 any pH value, useful buffer range: pH 9.7 – 11.1 sterile filtered | CAPSO – 0.5 M CSS-529 any pH value, useful buffer range: pH 9.0 – 10.3 sterile filtered | CHES – 1 M CSS-506 any pH value, useful buffer range: pH 8.6 – 10.0 sterile filtered |
| Citric Acid – 1 M CSS-508 any pH value, useful buffer range: pH 2.2 – 6.5 sterile filtered | DL-Malic Acid – 1 M CSS-509 any pH value, useful buffer range: pH 2.7 – 6.0 sterile filtered | Formic Acid – 1 M CSS-530 any pH value, useful buffer range: pH 3.0 – 4.5 sterile filtered |
| Glycine – 1 M CSS-510 any pH value, useful buffer range: pH 2.2 – 3.6 and pH 8.6 – 10.6 sterile filtered | HEPES – 1 M CSS-511 any pH value, useful buffer range: pH 6.8 – 8.2 sterile filtered | Imidazole – 1 M CSS-512 any pH value, useful buffer range: pH 6.2 – 7.8 sterile filtered |
| Lithium Acetate – 1 M CSS-513 any pH value, useful buffer range: pH 3.6 – 5.6 sterile filtered | MES – 1 M CSS-514 any pH value, useful buffer range: pH 5.5 – 6.7 sterile filtered | MOPS – 1 M CSS-515 any pH value, useful buffer range: pH 6.5 – 7.9 sterile filtered |
| PIPES – 1 M CSS-516 any pH value, useful buffer range: pH 6.5 – 7.5 sterile filtered | Potassium Phosphate – 1 M CSS-517 any pH value, useful buffer range: pH 5.8 – 8.0 sterile filtered | Potassium Phosphate Citrate – 1 M CSS-507 any pH value, useful buffer range: pH 2.6 – 7.0 sterile filtered |
| Sodium Acetate (HCl) – 1 M CSS-518 any pH value, useful buffer range: pH 3.6 – 5.6 sterile filtered | Sodium Acetate – 1 M CSS-519 any pH value, useful buffer range: pH 3.6 – 5.6 sterile filtered | Sodium Citrate – 1 M CSS-526 any pH value, useful buffer range: pH 5.0 – 6.2 sterile filtered |
| Sodium Phosphate – 1 M CSS-520 any pH value, useful buffer range: pH 5.8 – 8.0 sterile filtered | Sodium Phosphate Citrate – 1 M CSS-531 any pH value, useful buffer range: pH 2.6 – 7.0 sterile filtered | Sodium Potassium Phosphate – 1 M CSS-521 any pH value, useful buffer range: pH 5.8 – 8.0 sterile filtered |
| Succinic Acid – 0.5 M CSS-522 any pH value, useful buffer range: pH 3.2 – 6.5 sterile filtered | TAPS – 1 M CSS-532 any pH value, useful buffer range: pH 7.7 – 9.1 sterile filtered | Tricine – 1 M CSS-523 any pH value, useful buffer range: pH 7.4 – 8.8 sterile filtered |
| TRIS (TRIS-Acetate) – 1 M CSS-524 any pH value, useful buffer range: pH 7.0 – 9.0 sterile filtered | TRIS – 1 M CSS-525 any pH value, useful buffer range: pH 7.0 – 9.0 sterile filtered |
Crystallization stock solutions, i.e. polymers, buffers and salts are ideal for the optimization of your crystallization conditions.
Using the same chemicals as utilized in the JBScreens ensures higher reproducibility of your experiments. Crystallization Stock Solutions are ready for use: the concentration is adjusted and most of them are sterile filtered.
Super Buffers screen the pH independently from any other parameter. They are composed of a mixture of three individual buffers with distinct pKa values and cover a broad pH range without changing the chemical environment of the buffer solution[1].
Our Super Buffers are supplied as low and high pH stock solutions, which can be mixed at different ratios to obtain different pH values within the range. Plotting the pH vs. the percentage of high pH stock solution in the mixture results in an almost linear pH function for any JBScreen Super Buffer system.
| Products & Ordering | ||
| AAB pH 4.0 – 1 M CSS-404 Buffer System: Sodium Acetate, ADA, Bicine sterile filtered | AAB pH 9.0 – 1 M CSS-405 Buffer System: Sodium Acetate, ADA, Bicine sterile filtered | CHC pH 4.0 – 1 M CSS-402 Buffer System: Citric Acid, HEPES, CHES sterile filtered |
| CHC pH 10.0 – 1 M CSS-403 Buffer System: Citric Acid, HEPES, CHES sterile filtered | MIB pH 4.0 – 1 M CSS-400 Buffer System: Malonic Acid, Imidazole, Boric Acid sterile filtered | MIB pH 10.0 – 1 M CSS-401 Buffer System: Malonic Acid, Imidazole, Boric Acid sterile filtered |
| MMT pH 4.0 – 1 M CSS-398 Buffer System: DL Malic Acid, MES and TRIS sterile filtered | MMT pH 9.0 – 1 M CSS-399 Buffer System: DL Malic Acid, MES and TRIS sterile filtered | PCB pH 4.0 – 1 M CSS-387 Buffer System: Sodium Propionate, Sodium Cacodylate and BIS-TRIS Propane sterile filtered |
| PCB pH 9.0 – 1 M CSS-388 Buffer System: Sodium Propionate, Sodium Cacodylate and BIS-TRIS Propane sterile filtered | SPG pH 4.0 – 1 M CSS-389 Buffer System: Succinic Acid, Sodium Dihydrogen Phosphate and Glycine sterile filtered | SPG pH 10.0 – 1 M CSS-390 Buffer System: Succinic Acid, Sodium Dihydrogen Phosphate and Glycine sterile filtered |
| TBG pH 4.0 – 1 M CSS-384 Buffer System: Sodium Tartrate Dihydrate, BIS-TRIS and Glycylglycine sterile filtered | TBG pH 9.0 – 1 M CSS-385 Buffer System: Sodium Tartrate Dihydrate, BIS-TRIS and Glycylglycine sterile filtered | TACS MMF pH 7.0 – 100 % CSS-420 Buffer System of 7 different organic acid salts |
Crystallization stock solutions, i.e. polymers, buffers and salts are ideal for the optimization of your crystallization conditions.
Using the same chemicals as utilized in the JBScreens ensures higher reproducibility of your experiments. Crystallization Stock Solutions are ready for use: the concentration is adjusted and most of them are sterile filtered.
| Products & Ordering | |||
| Ammonium Acetate – 5 M CSS-129 sterile filtered | Ammonium Bromide – 3 M CSS-423 sterile filtered | Ammonium Chloride – 5 M CSS-131 sterile filtered | Nickel Sulfate Hexahydrate – 1 M CSS-227 sterile filtered |
| Ammonium dihydrogen Phosphate – 3 M CSS-133 sterile filtered | Ammonium Fluoride – 10 M CSS-134 sterile filtered | Ammonium Formate – 5 M CSS-136 sterile filtered | Nickel(II) Chloride Hexahydrate – 1 M CSS-228 sterile filtered |
| Ammonium Iodide – 1 M CSS-137 sterile filtered | Ammonium Nitrate – 10 M CSS-138 sterile filtered | Ammonium Sulfate – 4 M CSS-143 sterile filtered | Potassium Acetate – 5 M CSS-262 sterile filtered |
| Cadmium Chloride – 1 M CSS-151 sterile filtered | Cadmium Sulfate – 1 M CSS-152 sterile filtered | Calcium Acetate Hydrate – 1 M CSS-153 sterile filtered | Potassium Bromide – 4 M CSS-264 sterile filtered |
| Calcium Chloride Dihydrate – 5 M CSS-155 sterile filtered | Cesium Chloride – 1 M CSS-157 sterile filtered | Cobalt(II) Chloride Hexahydrate – 1 M CSS-163 sterile filtered | Potassium Chloride – 4 M CSS-371 sterile filtered |
| di-Ammonium hydrogen Phosphate – 3.5 M CSS-171 sterile filtered | di-Ammonium Tartrate – 2 M CSS-172 sterile filtered | di-Potassium hydrogen Phosphate – 1 M CSS-391 sterile filtered | Potassium dihydrogen Phosphate – 1 M CSS-268 sterile filtered |
| di-Sodium hydrogen Phosphate – 1 M CSS-392 sterile filtered | Hexadecyltrimethylammonium Bromide – 0.05 M CSS-395 Cetyltrimethylammonium bromide sterile filtered | Iron (III) Chloride Hexahydrate – 1 M CSS-184 sterile filtered | Potassium Formate – 10 M CSS-269 sterile filtered |
| Lithium Chloride – 10 M CSS-356 sterile filtered | Lithium Citrate Hydrate – 1.5 M CSS-203 sterile filtered | Lithium Nitrate – 8 M CSS-204 sterile filtered | Potassium Iodide – 1 M CSS-270 sterile filtered |
| Lithium Sulfate – 2.5 M CSS-207 sterile filtered | Magnesium Acetate Tetrahydrate – 1 M CSS-210 sterile filtered | Magnesium Chloride Hexahydrate – 1 M CSS-211 sterile filtered | Potassium L-Tartrate Monobasic – 0.025 M CSS-271 sterile filtered |
| Magnesium Formate Dihydrate – 1 M CSS-393 sterile filtered | Magnesium Nitrate Hexahydrate – 1 M CSS-214 sterile filtered | Magnesium Sulfate Heptahydrate – 2.5 M CSS-216 sterile filtered | Potassium Nitrate – 1 M CSS-272 sterile filtered |
The Thermofluor Screens JBScreen FUNDAMENT and JBScreen SPECIFIC allow identification of protein-stabilizing buffer conditions which is pivotal for protein purification, characterization and crystallization.
Undesired overlay of screening of interdependent variables is prevented by strictly categorizing stability screening of proteins into
1. FUNDAMENTAL factors that influence the whole protein molecule (pH and ionic strength)
2. SPECIFIC factors that affect energetically important hot spots on the protein (substrates and their analogs, cations, anions, …)
The protein’s melting temperature (Tm) is used as reporter for protein stability and determined by a thermal shift assay (96-well plate format) monitoring the unfolding of a protein in a temperature-dependent manner. The higher the Tm, the higher is the thermostability of the protein in that specific environment.
JBScreen Thermofluor FUNDAMENT and SPECIFIC are provided in a deep-well block at 0.5 ml each, which allows a flexible application of this alternative approach.
α-Chymotrypsinogen A was applied in JBScreen Thermofluor FUNDAMENT and SPECIFIC.
Stabilizing conditions (high ionic strength, neutral pH, CaCl2 & FeCl3) were combined without further optimization. A crystallization screen was set up:
Crystal growth was promoted by the stabilizing specific ions CaCl2 & FeCl3 from JBScreen Thermofluor SPECIFIC.
| Products & Ordering |
| JBScreen Thermofluor FUNDAMENT CS-332 Thermal Shift Assay for protein stability |
| JBScreen Thermofluor SPECIFIC CS-333 Thermal Shift Assay for protein stability |
| JBS Thermofluor Dye X-TD |
The JBS Solubility Kit is a pre-crystallization screen to improve the composition of the initial protein buffer solution prior to performing crystallization set-ups [1]. Since the highly complex properties of proteins are dependent on their environment, buffer solutions play an important role, i.e. influencing the solubility and the aggregation behaviour of the protein sample.
Studies have shown that aggregation of the protein may inhibit nucleation and crystal growth. Therefore, the JBS Solubility Kit has been developed to investigate protein samples towards their homogeneity and monodispersity prior to crystallization trials, employing hanging drop vapour diffusion experiments combined with dynamic light scattering.
The JBS Solubility Kit contains a set of 24 buffer solutions at different pH-values for setting up hanging drop vapour diffusion experiments in order to monitor the aggregation and precipitation of the protein sample, and a set of 14 additives used for further optimization employing dynamic light scattering.
| Products & Ordering |
| JBS Solubility Kit CO-310 |
[1] Jancarik et al. (2004) Optimum solubility (OS) screening: an efficient method to optimize buffer conditions for homogeneity and crystallization of proteins. Acta Cryst D 60:1670.
JBScreen Solubility HTS, developed by Meindert Lamers from the MRC in Cambridge, is designed to quickly find suitable buffer components to purify and store protein in.
JBScreen Solubility HTS tests for buffer, pH, salt and glycerol at the same time: For all proteins investigated, suitable conditions were found in a single assay. Protein and buffer conditions are dispensed in a ratio of 1:3, thereby minimizing the effect of any buffer components in which the protein is initially stored. Standard crystallization robots set up the assay in 5 minutes and very small amounts of protein are required (10 µl @ 5-10 mg/ml). The results are visible after one hour at high protein concentration or 12 hours at low protein concentration:
Examples of a drop without protein precipitation (left) and a drop with protein precipitation (right)
Manual JBScreen Solubility HTS
| Products & Ordering |
| JBScreen Solubility HTS CO-311 |
JBScreen Detergents contain 4 x 24 unique detergents that are compatible with most common crystallization reagents and are therefore perfectly suited for membrane protein solubilization:
JBScreen Detergents can be used throughout the protein purification process or can be added afterwards by dialysis or ion-exchange chromatography (detergent exchange). Detergent exchange can be vital for obtaining well-diffracting membrane-protein crystals [1].
JBScreen Detergents is also valuable for additive screening with detergents and detergent mixtures [2,3] in combination with the JBScreen Membrane. This combination will enable you to screen a broad range of detergents, while concentrating on the most successful crystallization conditions, making crystallization screening of membrane proteins much more efficient and less time consuming.
Screen for stabilizing detergents by combining JBScreen Detergents with Prometheus NT.48, a label-free nanoDSF technology developed by NanoTemper Technologies, ideally suited for membrane protein stabilization.
NanoTemper Application Note: Thermal Unfolding of Membrane Proteins
| Products & Ordering | ||
| JBScreen Detergents 1 CS-521 | JBScreen Detergents 3 CS-523 | JBScreen Detergents HTS CS-525 |
| JBScreen Detergents 2 CS-522 | JBScreen Detergents 4 CS-524 | JBScreen Membrane 1 – 4 & JBScreen Detergents HTS CS-308 |
[1] Rosenow et al. (2003) The influence of detergents and amphiphiles on the solubility of the light harvesting complex. Acta Cryst. D59:1422
[2] Adir (1999) Crystallization of the oxygen-evolving reaction centre of photosystem II in nine different detergent mixtures. Acta Cryst. D55:891
[3] Koronakis et al. (2000) Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405:914
JBScreen Plus is an additive screen most useful in the optimization of preliminary crystallization conditions. The selection of the additives is based on the Hofmeister series, which reflects the ability of ions to stabilize the structure of proteins. Thus ions can be classified as either kosmotropic or chaotropic. The first having structure stabilizing properties, thus they may assist in, e.g. crystallizing proteins with a high proportion of flexible loop regions. The latter show structure disturbing properties which may assist in the crystallization of large complexes allowing them to re-arrange to form favorable crystal contacts.
JBScreen Plus consists of 5 individual kits, JBScreen Plus Kosmotropic, JBScreen Plus Chaotropic, JBScreen Plus Salts, JBScreen Plus Additives and JBScreen Plus Volatiles, containing 24 different additives each. The ready-to-use reagents are supplied in 1 ml aliquots.
The 96 solutions of JBScreen Plus HTS, comprising the reagents of the kosmotropic, chaotropic, salts and additive kit, are supplied in a sterile deep well block containing 1 ml per well.
| Products & Ordering | |
| JBScreen Plus Kosmotropic CS-501 | JBScreen Plus Volatiles CS-505 |
| JBScreen Plus Chaotropic CS-502 | JBScreen Plus Complete CS-506 all 5 JBScreen Plus kits for a special price |
| JBScreen Plus Salts CS-503 | JBScreen Plus HTS CS-507L |
| JBScreen Plus Additives CS-504 |
Common buffers at 0.5 M concentration provided in a deep well block (1.7 ml of each condition).
Choose between JBScreen Buffers (neutral pH range from 5.5 – 8.5) and JBScreen Buffers Xtreme (extreme pH ranges from 3.0 – 5.5 and 8.5 – 11.0).
Suitable as follow-up screens for JBScreen Thermofluor or as standard buffer screens.
| Products & Ordering | |
| JBScreen Buffers CS-214 | JBScreen Buffers Xtreme CS-215 |
Get your protein ready for crystallization! Consider to alter the protein surface or modify the sequence by truncation or mutagenesis. Or try a new mode of production.
Surface engineering of proteins can be a powerful technique for dealing with proteins that yield no or poorly diffracting crystals. In particularly, reductive methylation of proteins has emerged as a standard procedure in several large scale facilities and research programs, i.e. the Midwest Centre of Structural genomics [1] and the Structural Proteomics In Europe (SPINE) program [2,3].
The JBS Methylation Kit is designed for selective methylation of lysine residues. The method does not require laborious cloning/expression/purification but chemically replaces the protons of the amino group of all lysine residues with methyl groups. The result is a surface-engineered protein within 24 hours ready for crystallization.
Each JBScreen Methylation Kit contains all necessary reagents for six methylation experiments. All components are provided ready for use. Just follow the manual step-by-step. No background in chemistry necessary.
| Products & Ordering |
| JBS Methylation Kit CS-510 |
[1] Kim et al. (2008) Large-scale evaluation of protein reductive methylation for improving protein crystallization. Nature Methods 5:853.
[2] Fogg et al. (2006) Application of the use of high-throughput technologies to the determination of protein structures of bacterial and viral pathogens. Acta Cryst. D 62:1196.
[3] Walter et al. (2006) Lysine methylation as a routine rescue strategy for protein crystallization. Structure 14:1617.
JBS Floppy-Choppy is the rescue kit for proteins which are recalcitrant to crystallization. It enables the researcher to modify the protein target by in situ proteolysis to improve its crystallization behavior .
The method implies the addition of trace amounts of protease to the protein solution immediately prior to crystallization. Thus, the crystallization experiment is very straightforward. It can be set up without evaluating the efficacy of proteolysis, without stopping the proteolysis reaction and without purification of any proteolyzed protein fragments.
In situ proteolysis is one of the most efficacious crystallization rescue strategies used at structural genomic centers [1,2].
| Products & Ordering |
| JBS Floppy-Choppy CO-110 In situ proteolysis as rescue technique in protein crystallization |
[1] Dong et al. (2007) In situ proteolysis for protein crystallization and structure determination. Nature Methods 4:1019.
[2] Wernimont et al. (2009) In Situ Proteolysis to Generate Crystals for Structure Determination: An Update. PLoS ONE 4:e5094
Protein Crystallization Rescue Strategies
Do not discard bad diffracting crystals! They can be very useful, too. Try to improve diffraction by crystal annealing, varying the solvent content or use your initial crystals for seeding.
Crystal Annealing is a promising technique to improve diffraction quality of poorly diffracting protein crystals.
The Cryo Shutter, developed by Dr. Uwe Mueller et al., MX-Lab at BESSY-II, HZB Berlin-Adlershof, is designed for crystal annealing at home sources:
The Cryo Shutter Assembly Kit is available for Cryojet Systems (Oxford Instruments) as well as for Cryostream 700 Systems (Oxford Cryosystems).
Shutter operation requires a compressed air source!
| Products & Ordering | ||
| Cryo Shutter for Cryojet Systems CC-330-19 | Cryo Shutter for Cryojet Systems with limited space CC-330-19LTD | Cryo Shutter for Cryostream 700 Systems CC-330-22 |
Dehydration has been used as a tool for inducing structural changes in protein crystals since the earliest days of protein crystallography. Though neglected, dehydration remains a powerful tool for improving or at least modifying the diffraction properties of protein crystals.
Of all post-crystallization treatments, dehydration has proven to be the most effective in improving crystal diffraction properties. Of course, dehydration also often severely degrades crystal diffraction, but (amazingly!) original crystal order can usually be fully recovered just by rehydrating.
Dehydration Salts and the Crystal Dehydration and Salvage Kit have been designed for an easy, controlled and reliable way to dehydrate protein crystals and thus provide an efficient tool for altering / improving their diffraction properties.
The Dehydration Salts contain 12 saturated salt solutions, 1 ml each, producing relative humidities in the range of 22.5 to 97.3 %.
The Crystal Dehydration and Salvage Kit, shown on the left, is composed of the 12 dehydration salts, MiTeGen’s goniometer bases and RT Tubing.
The Crystal Dehydration and Salvage Kit (CO-122) is nonsaleable to USA and Japan! Please contact MiTeGen for distributor information.
| Products & Ordering | |
| Dehydration Salts CO-121 | Crystal Dehydration and Salvage Kit CO-122 |
Preparation of seed stocks from protein crystals for microseeding applications. A highly polished glass bead and a microcentrifuge tube are used as mortar and pestle for crushing of seed crystals.
24 glass beads, each in a 1.5 ml microcentrifuge tube.
Each glass bead is hardened and hilghly polished. The shape of the bottom of the microcentrifuge tube matches the shape of the bead to ensure effective crystal crushing.
JBS Beads-for-Seeds can be utilized to prepare seed stocks from protein crystals. Crystals and stabilizing solution are added to the highly polished glass bead in the microcentrifuge tube and the seed stock is generated simply by vortexing.
Adding a seeding solution to a crystallization experiment allows growing crystals in the metastable zone of the phase diagram. Further, the number and size of the crystals can be influenced by serial dilution of the seed stock [1].
[1] Luft et al. (1999) A method to produce microseed stock for use in the crystallization of biological macromolecules. Acta Cryst. D55:988.
| Products & Ordering |
| JBS Beads-for-Seeds CO-501 |
The patent-pending XtalTool was developed as a platform for protein X-ray crystallography to be used in all steps from crystallization, ligand soaking and data collection without any direct crystal handling. It is specially interesting therefore for fragile crystals, in which any manipulation might disturb crystal packing and impair diffraction quality.
XtalTools replace regular cover slides used in hanging drop 24 well plates without compromising on optical parameters since crystal growth can be monitored using a regular microscope. The design of XtalTool permits accurate addition and removal of ligand, fragment and/or cryoprotectant solutions without disturbance of the crystals. Once crystals are prepared to the individual user’s needs, XtalTool can be directly used to collect crystallographic diffraction data at room or cryogenic temperature. Its geometrical design allows high compatibility with most synchrotron and in-house beamlines as it shares the standard 18 mm SPINE length of a regular sample holder. The employed crystal supporting material is X-ray translucent and does not interfere with diffraction data collection.
XtalTool HT is a further development with the same general features as XtalTool, but with a modified geometry of the inner sample holder that can be broken free at predefined breakpoints. The remaining inner sample holder then fits into a SPINE standard magnetic CryoVial and thereby facilitates robot assisted sample mounting. XtalTool HT is available in two sizes (22 and 18 mm diameter) compatible with the two standard 24 well crystallization plate formats. Despite the different outer diameter, the geometry of the inner sample holder is identical.
| Products & Ordering | |
| XtalTool X-XT-101 Sample Holder for Crystal Growth, in situ Ligand Soaking and in situ Data Collection | XtalTool Soaking Kit X-XT-102 |
| XtalTool HT 22 mm X-XT-103 Sample Holder for Crystal Growth, in situ Ligand Soaking and in situ Data Collection with a Robot Assisted Sample Mounting | XtalTool HT 18 mm X-XT-104 Sample Holder for Crystal Growth, in situ Ligand Soaking and in situ Data Collection with a Robot Assisted Sample Mounting |
| XtalTool Bases X-XT-105 |
Shilova et al. (2020) Current status and future opportunities for serial crystallography at MAX IV Laboratory. J. Synchrotron Rad. 27:1095.
Feiler et al. (2019) An All-in-one Sample Holder for Macromolecular X-ray Crystallography with Minimal Background Scattering. J. Vis. Exp. 149:e59722.
Jena Bioscience distributes MiTeGen’s innovative crystallography products.
Correctly orienting your crystal relative to the X-ray beam and to the goniometer rotation axis is essential to maximizing data collection efficiency and minimizing radiation damage.
Some crystal morphologies regularly end up in non-optimum orientations.
For example, thin plates usual end up with their largest face adhered to the plane of the mount or loop. The thickness direction typically corresponds to the longest unit cell dimension. Diffraction spot overlap can result when this direction approaches the beam direction, especially if the crystal has appreciable mosaicity.
To provide a new level of crystal orientation control, MiTeGen now offers Angled-Tip versions of all of its MicroMounts, Loops and Meshes. The tip is angled relative to the rod and the rotation axis by 45, 60 or 90* degrees +/- 5 degrees. This ensures that the long-cell direction is always far from the incident X-ray beam direction for optimum data collection.
*Note that the increased bend angle of 90 degrees may present more of a challenge during crystal harvesting. This can be aided with use of a secondary mount or tool to help in positioning the crystal.
Angled-tip versions are generated from MiTeGen’s standard products as a custom service. Select the products you want, and then order the service below for each box you want modified, and all twenty (20) mounts will be adjusted to our angle specification.
Important note: Please clearly indicate the box you want modified!
| Products & Ordering | |
| Changed orientation of crystal mounts to 45 degree angle CA-45 modification to 1 box of 20 mounts/loops/meshes (mounts ordered separately) |
Changed orientation of crystal mounts to 90 degree angle CA-90 modification to 1 box of 20 mounts/loops/meshes (mounts ordered separately) |
If you’ve been using nylon loops for crystal harvesting and data collection, Mitegen’s collection of general purpose and specialized tools may be a bit overwhelming. To help introduce you to MiTegen’s product portfolio, a sampler kit of some of the most popular tools has been assorted.
Crystal Harvesting Sampler Kit 1 (MSK-1) contains 40 mounts for crystal harvesting and data collection on 18 mm SPINE rods:
Crystal Harvesting Sampler Kit 2 (MSK-2) contains 120 mounts for crystal harvesting and data collection on 18 mm SPINE rods:
| Products & Ordering | |
| Crystal Harvesting Sampler Kit 1 MSK-1 40 tools on 18 mm SPINE length pins |
Crystal Harvesting Sampler Kit 2 MSK-2 120 tools on 18 mm SPINE length pins |
Each box contains 24 MicroCrystal Mounts™ precision-attached to nonmagnetic SPINE standard pins.
These ultra-transparent mounts meet the challenges of visualizing, aligning, and collecting diffraction data from micron size crystals. Using dual-thickness technology, crystals are supported on a 3 micron thick film in a 10 micron thick frame. An aerodynamic design combined with a reduced tip length minimizes sample motion. MicroCrystal Mounts provide an unsurpassed combination of X-ray transparency and rigidity.
Specifically designed for:
Crystals are supported on a 3 μm thick film held in place by a 10 μm thick body, this provides for:
Each design is currently available in two versions: one with a smooth top surface and the 10 micron thick outer “rib” on the bottom surface, and one with the out rib projecting out on the upper surface.
| Products & Ordering |
| MicroCrystal Mount Assortment M4-L18SP-A1 2 each of model 1 – 12, SPINE length |
Each box contains 20 MicroGripper™ Mounts precision-attached to nonmagnetic SPINE standard pins.
MicroGripper™ Mounts provide a new approach to retrieving and mounting crystals for room and low temperature measurements.
With all conventional mounts, protein and virus crystals are held in contact with the mount by liquid capillary forces at room temperature, and by frozen liquid at cryogenic temperatures. “Dry” crystals, which give the lowest possible background scatter, tend to fall off the mount.
With a MicroGripper™ Mount, you simply push the mount down onto your crystal. Its tiny, flexible, soft fingers then gently grab your crystal without damaging it (yes, even for protein and virus crystals), firmly holding your crystal in place.
MicroGrippers™ are ideal for data collection at and near room temperature. Because the crystal is gripped, viscous oils are no longer needed to prevent crystal slippage during rotations. Crystals can be mounted at home and shipped to the synchrotron at room temperature.
Use MicroGrippers™ with MiTeGen’s MicroRT™ system for easy and foolproof room-temperature data collection. For the lowest background scatter possible, wick away all surrounding liquid before gripping your crystal, and then rehydrate it within the MicroRT tube by injecting a small amount of mother liquor down toward the sealed end of the tube.
MicroGrippers are also well suited for thin plates and rods. Slip them under your crystal, and their soft, flexible fingers will provide very gentle support for the most fragile samples.
For all sizes, the distance from the pin base to the center of the crystal aperture is precisely 18.5 mm and compatible with the SPINE standard. The length tolerance of the pins is 0.3 mm only.
Pins are marked in 2 mm increments and can be cut to a desired length using spring steel compatible cutters.
They are compatible with all standard X-ray hardware, and can be inserted in 0.7 mm mechanical pencils or micromanipulators for easy handling.
Cleaning Instruments for MicroMounts etc.
| Products & Ordering | |
| MicroGripper Mounts – Assortment M7-L18SP-A1 5 each of 50, 100, 200, and 300 µm aperture MicroGrippers, SPINE length |
50 µm aperture MicroGripper Mounts M7-L18SP-50 SPINE length |
| 100 µm aperture MicroGripper Mounts M7-L18SP-100 SPINE length |
200 µm aperture MicroGripper Mounts M7-L18SP-200 SPINE length |
| 300 µm aperture MicroGripper Mounts M7-L18SP-300 SPINE length |
Please note: Other pin lengths, i.e. L11, L19 and L25, will be available upon request but may have significant lead times.
Each box contains 20 Indexed MicroMesh mounts, attached to solid nonmagnetic stainless steel pins.
Indexed MicroMesh™ Mounts have all the features and advantages of regular MicroMesh™ Mounts for microcrystal crystallography and diffraction measurements, including the smallest background scatter of any commercial mount, and a sieve-like action that allows easy retrieval of sub-30 μm crystals.
Indexing makes it easier to locate (and then to relocate) a given crystal on the mount. Identify the most promising crystals on your home microscope, and then easily find them again on your microfocus source. Do a high magnification search at the beamline and then refind and shoot the best crystal, without having to zoom out.
Microcrystals from a given drop often have more than one crystalline form/packing, and the different forms may diffract to very different resolutions. Use high magnification to identify and shoot these different forms.
Three styles of indexed MicroMesh mounts, all with 25 μm mesh openings are offered.
The first two are based on MiTeGen’s popular 400/25 MicroMesh Mount. The mesh area is divided into four quadrants, and additional diagonal tabs allow the front/back orientation of the mesh and a crystal’s position on the mesh to be uniquely determined in only a 100 μm field of view. In style 400/25-IN1, the quadrants are numbered. In style 400/25-IN2, the numbers are replaced by 60 μm square apertures. Crystals suspended across these larger apertures can sometimes be easier to see.
The third style has a 300 μm mesh area divided into nine numbered 100 μm areas. The flat top of this mount makes it easier to scrape/scoop crystals off of the bottom of a well or coverslip.
For all sizes, the distance from the pin base to the center of the crystal aperture is precisely 18.5 mm and compatible with the SPINE standard. The length tolerance of the pins is 0.3 mm only.
Pins are marked in 2 mm increments and can be cut to a desired length using spring steel compatible cutters.
They are compatible with all standard X-ray hardware, and can be inserted in 0.7 mm mechanical pencils or micromanipulators for easy handling.
Cleaning Instructions for MicroMounts etc.
| Products & Ordering | ||
| Indexed MicroMesh™ Mounts – 400/25-IN1 M3-L18SP-400-IN1 20 of 400 micron diameter, 25 micron aperture meshes SPINE length | Indexed MicroMesh™ Mounts – 400/25-IN2 M3-L18SP-400-IN2 20 of 400 micron diameter, 25 micron aperture meshes SPINE length | Indexed MicroMesh™ Mounts – 300/25-IN1 M3-L18SP-300-IN1 20 of 300 micron diameter, 25 micron aperture meshes SPINE length |
Please note: Other pin lengths, i.e. L11, L19 and L25, will be available upon request but may have significant lead times.
Each box contains 20 MicroMesh™ Mounts precision-attached to nonmagnetic SPINE standard pins.
MicroMesh™ Mounts are the tool of choice for microcrystal crystallography and diffraction experiments, especially at microfocus beamlines. They have been used in de novo protein structure determination from crystals as small as 5 μm.
They are excellent for rod shaped crystals, and in particular are superior to mounts with elliptical apertures, because the mesh provides continuous, gentle support for rods of all sizes.
MicroMeshes produce the smallest background scatter of any commercial mount. Their sieve-like action allows easy retrieval of sub-30 μm crystals.
We offer five different size MicroMeshes. All are 10 μm thick and are curved around the same nonmagnetic stainless steel pins used for MicroMounts, producing the same scoop-like action.
The first three have a 400 μm mesh area with openings of 10, 25 and 50 μm, respectively. The fourth has a 700 μm diameter mesh area with 25 μm openings. The fifth MicroMesh Mount has an 80 μm diameter mesh area with 15 μm openings.
For all sizes, the distance from the pin base to the center of the crystal aperture is precisely 18.5 mm and compatible with the SPINE standard. The length tolerance of the pins is 0.3 mm only.
Pins are marked in 2 mm increments and can be cut to a desired length using spring steel compatible cutters.
They are compatible with all standard X-ray hardware, and can be inserted in 0.7 mm mechanical pencils or micromanipulators for easy handling.
| Products & Ordering | |
| MicroMesh™ Mounts – Assortment M3-L18SP-A1 5 each of 400/10, 400/25, 400/50 and 700/25 µm meshes SPINE length | MicroMesh™ Mounts – 400/10 M3-L18SP-10 20 of 400 micron diameter, 10 micron aperture meshes SPINE length |
| MicroMesh™ Mounts – 400/25 M3-L18SP-25 20 of 400 micron diameter, 25 micron aperture meshes SPINE length | MicroMesh™ Mounts – 400/50 M3-L18SP-50 20 of 400 micron diameter, 50 micron aperture meshes SPINE length |
| MicroMesh™ Mounts – 700/25 M3-L18SP-25L 20 of 700 micron diameter, 25 micron aperture meshes SPINE length | MicroMesh™ Mounts – 80/15 M3-L18SP-15 20 of 80 micron diameter, 15 micron aperture meshes SPINE length |
Please note: Other pin lengths, i.e. L11, L19 and L25, will be available upon request but may have significant lead times.
Each box contains 20 MicroLoops E™ precision-attached to nonmagnetic SPINE standard pins.
The elongated sample apertures of the MicroLoops E™ are particularly suitable for needle or rodshaped samples. You can choose between Vertical, Horizontal and Inclined aperture MicroLoops E™.
The small fingers projecting into the aperture gently support your sample. Use the inclined apertures to improve crystal orientation for the most efficient data collection.
For all sizes, the distance from the pin base to the center of the crystal aperture is precisely 18.5 mm and compatible with the SPINE standard. The length tolerance of the pins is 0.3 mm only. They are compatible with all standard X-ray hardware, and can be inserted in 0.7 mm mechanical pencils or micromanipulators for easy handling.
| Products & Ordering | |
| Vertical MicroLoops E – Assortment M8-L18SP-VA1 5 each of 15×150, 30×300, 50×500 and 70×700 µm aperture, SPINE length | Horizontal MicroLoops E – Assortment M8-L18SP-HA1 10 each of 15×150 and 50×500 µm aperture, SPINE length |
| Inclined MicroLoops E – Assortment M8-L18SP-IA1 10 each of 15×150 and 50×500 µm aperture, SPINE length | Horizontal MicroLoops E M8-L18SP-15H 20 each of 15×150 µm aperture, SPINE length |
| Horizontal MicroLoops E M8-L18SP-50H 20 each of 50×500 µm aperture, SPINE length | Inclined MicroLoops E M8-L18SP-15I 20 each of 15×150 µm aperture, SPINE length |
| Inclined MicroLoops E M8-L18SP-50I 20 each of 50×500 µm aperture, SPINE length | Vertical MicroLoops E M8-L18SP-15V 20 each of 15×150 µm aperture, SPINE length |
| Vertical MicroLoops E M8-L18SP-30V 20 each of 30×300 µm aperture, SPINE length | Vertical MicroLoops E M8-L18SP-50V 20 each of 50×500 µm aperture, SPINE length |
| Vertical MicroLoops E M8-L18SP-70V 20 each of 70×700 µm aperture, SPINE length |
Please note: Other pin lengths, i.e. L11, L19 and L25, will be available upon request but may have significant lead times.
Each box contains 20 Dual-Thickness MicroLoop LD™ precision-attached to nonmagnetic SPINE standard pins.
Dual-Thickness MicroLoops LD have a computer-optimized design with longer, thinner necks to minimize disturbance when inserted and withdrawn from small liquid drops. Thick polymer in the neck region makes these mounts rigid in, e.g., a cold gas stream, and thin polymer in the loop region ensures the lowest possible background scatter in X-ray diffraction applications. The world’s most advanced loop design.
Dual-Thickness MicroLoops LD have aperture sizes of 20, 35, 50, 75, 100, 150, 200 and 300 μm.
For all sizes, the distance from the pin base to the center of the crystal aperture is precisely 18.5 mm and compatible with the SPINE standard. The length tolerance of the pins is 0.3 mm only.
Pins are marked in 2 mm increments and can be cut to a desired length using spring steel compatible cutters.
They are compatible with all standard X-ray hardware, and can be inserted in 0.7 mm mechanical pencils or micromanipulators for easy handling.
| Products & Ordering | |
| DT MicroLoops LD – Small Aperture Assortment M5-L18SP-A1LD 5 each of 20, 35, 50 and 75 µm aperture loops, SPINE length | DT MicroLoops LD – Medium Aperture Assortment M5-L18SP-A2LD 5 each of 100, 150, 200 and 300 µm aperture loops, SPINE length |
| 20 µm aperture DT MicroLoops LD M5-L18SP-20LD SPINE length | 35 µm aperture DT MicroLoops LD M5-L18SP-35LD SPINE length |
| 50 µm aperture DT MicroLoops LD M5-L18SP-50LD SPINE length | 75 µm aperture DT MicroLoops LD M5-L18SP-75LD SPINE length |
| 100 µm aperture DT MicroLoops LD M5-L18SP-100LD SPINE length | 150 µm aperture DT MicroLoops LD M5-L18SP-150LD SPINE length |
| 200 µm aperture DT MicroLoops LD M5-L18SP-200LD SPINE length | 300 µm aperture DT MicroLoops LD M5-L18SP-300LD SPINE length |
Please note: Other pin lengths, i.e. L11, L19 and L25, will be available upon request but may have significant lead times.
Each box contains 20 Dual-Thickness MicroLoops™ precision-attached to nonmagnetic SPINE standard pins.
DT MicroLoops™ provide a superior tool in a familiar format for manipulating and mounting protein/small molecule crystals and many other small fragile samples.
They have circular sample aperture sizes of 50, 100, 150, 200, 300, 400, 500, 600, 800 and 1000 μm, available in single size boxes and 3 different assortments:
Compared with conventional nylon loop mounts and with competing lithographically fabricated mylar loop mounts,
DT MicroLoops™ provide:
For all sizes, the distance from the pin base to the center of the crystal aperture is precisely 18.5 mm and compatible with the SPINE standard. The length tolerance of the pins is 0.3 mm only. DT MicroLoops™ are compatible with all standard X-ray hardware, and can be inserted in 0.7 mm mechanical pencils or micromanipulators for easy handling.
| Products & Ordering | |
| DT MicroLoops – Medium Aperture Assortment M5-L18SP-A4 5 each of 50, 100, 150 and 200 µm aperture loops, SPINE length | DT MicroLoops – Large Aperture Assortment M5-L18SP-A5 5 each of 300, 400, 500 and 600 µm aperture loops, SPINE length |
| DT MicroLoops – Extra-Large Aperture Assortment M5-L18SP-A6 10 each of 800 and 1000 µm aperture loops, SPINE length | 50 µm aperture DT MicroLoops M5-L18SP-50 SPINE length |
| 100 µm aperture DT MicroLoops M5-L18SP-100 SPINE length | 150 µm aperture DT MicroLoops M5-L18SP-150 SPINE length |
| 200 µm aperture DT MicroLoops M5-L18SP-200 SPINE length | 300 µm aperture DT MicroLoops M5-L18SP-300 SPINE length |
| 400 µm aperture DT MicroLoops M5-L18SP-400 SPINE length | 500 µm aperture DT MicroLoops M5-L18SP-500 SPINE length |
| 600 µm aperture DT MicroLoops M5-L18SP-600 SPINE length | 800 µm aperture DT MicroLoops M5-L18SP-800 SPINE length |
| 1000 µm aperture DT MicroLoops M5-L18SP-1000 SPINE length |
Please note: Other pin lengths, i.e. L11, L19 and L25, will be available upon request but may have significant lead times.
Each box contains 20 Dual-Thickness MicroMounts™ precision-attached to nonmagnetic SPINE standard pins.
Utilizing advanced proprietary micro-fabrication processes, the Dual-Thickness MicroMounts have a thick, semi-rigid body and a thin, highly X-ray transparent crystal-receiving aperture. This dual thickness maximizes durability and rigidity, while maintaining the ultra-low X-ray background scatter that original MicroMounts™ are known for.
They are compatible with all standard X-ray hardware, and can be inserted in 0.7 mm mechanical pencils or micromanipulators for easy handling.
| Products & Ordering | |
| Small Aperture Assortment DT MicroMounts M2-L18SP-A1 5 each of 10, 20, 30 and 50 µm crystal apertures, SPINE length | Medium Aperture Assortment DT MicroMounts M2-L18SP-A2 5 each of 75, 100, 150 and 200µm crystal apertures, SPINE length |
| 10 µm aperture DT MicroMounts M2-L18SP-10 SPINE length | 20 µm aperture DT MicroMounts M2-L18SP-20 SPINE length |
| 30 µm aperture DT MicroMounts M2-L18SP-30 SPINE length | 50 µm aperture DT MicroMounts M2-L18SP-50 SPINE length |
| 75 µm aperture DT MicroMounts M2-L18SP-75 SPINE length | 100 µm aperture DT MicroMounts M2-L18SP-100 SPINE length |
| 150 µm aperture DT MicroMounts M2-L18SP-150 SPINE length | 200 µm aperture DT MicroMounts M2-L18SP-200 SPINE length |
Please note: Other pin lengths, i.e. L11, L19 and L25, will be available upon request but may have significant lead times.
Jena Bioscience distributes MiTeGen’s innovative crystallography products.
MiTeGen’s patent-pending MicroTools™ have tips made from soft, flexible microfabricated polymer films. The curvature of the tips gives them rigidity, but they can still easily be flexed to, e.g., slide flat along the well bottom in a multiwell plate, simplifying sample retrieval. These tools are far less likely to damage fragile samples than metal microtools, and are optically and X-ray transparent. Use for protein crystals, single cells and other small samples.
Each tool is mounted on a 0.025″/ 0.64 mm diameter nonmagnetic solid stainless steel rod.
The MicroTool™ Starter Kits contain additional tools to easily handle the MicroTools™ for crystal manipulation.
MicroTool™ Kit 1, the original kit, contains 20 tools for common sample manipulation tasks. These include dislodging samples from slides and plates separating samples, holding and transferring samples during soaks, rigidly holding samples at room temperature, cutting protein skins, gels and lipid phases, and measuring sample dimensions. The polymer film is 12.5 micrometers thick and produces little background X-ray scatter, so you can also use these tools to hold your sample in an X-ray beam.
MicroTool™ Kit 2 contains 20 tools for common sample manipulation tasks. The tips of these tools are 18 micrometers thick. This makes them more durable and rigid, but also increases background X-ray scatter.
MicroTool™ Kit 3 contains 20 tools for sample measurements. Two tool designs allow measurement of linear sample dimensions, and two allow measurement of both linear and angular dimensions. Use them to accurately measure small and fragile samples, including those contained in optically distorting liquid drops.
| Products & Ordering | |
| MicroTools™ Starter Kit 1 T1SK-1 MicroTools Kit 1 on 25 mm rods, preloaded into reusable B5 magnetic bases | MicroTools™ Starter Kit 2 T2SK-1 MicroTools Kit 2 on 25 mm rods, preloaded into reusable B5 magnetic bases |
| MicroTools™ Starter Kit 3 T3SK-1 MicroTools Kit 3 on 25 mm rods, preloaded into reusable B5 magnetic bases | MicroTools™ Kit 1-25 T1-L25-A1 25 mm pin lengths Assortment of 20 tools |
| MicroTools™ Kit 2-25 T2-L25-A1 25 mm pin lengths Assortment of 20 tools | MicroTools™ Kit 3-25 T3-L25-A1 25 mm pin lengths Assortment of 20 tools |
| Products & Ordering | |
| MicroTools™ Starter Kit 1 T1SK-1 MicroTools Kit 1 on 25 mm rods, preloaded into reusable B5 magnetic bases | MicroTools™ Starter Kit 2 T2SK-1 MicroTools Kit 2 on 25 mm rods, preloaded into reusable B5 magnetic bases |
| MicroTools™ Starter Kit 3 T3SK-1 MicroTools Kit 3 on 25 mm rods, preloaded into reusable B5 magnetic bases | MicroTools™ Kit 1-25 T1-L25-A1 25 mm pin lengths Assortment of 20 tools |
| MicroTools™ Kit 2-25 T2-L25-A1 25 mm pin lengths Assortment of 20 tools | MicroTools™ Kit 3-25 T3-L25-A1 25 mm pin lengths Assortment of 20 tools |
Jena Bioscience distributes MiTeGen’s innovative crystallography products.
Goniometer bases (sometimes called “caps”) are used to hold MicroMounts™, MicroLoops™, MicroMeshes™ and MicroGrippers™ in X-ray crystallography and related applications. The stainless steel rod of these products fits into the central hole of the base.
MiTeGen’s bases are compatible with standard cryo tools, with MiTeGen’s Magnetic CryoVials and all other commercial cryovials, with all magnetic goniometer head mounts and sample automounting hardware, and with loop sample mounts from other manufacturers.
Unlike other available bases, our patented designs tightly capture the MicroRT™ capillaries to allow easy and seamless room-temperature and low-temperature data collection.
We offer several designs to ensure compatibility with both protein and small molecule crystallography hardware and with all sample automounters.
The eco-friendly and patent-pending designs grab and securely hold MicroMounts™, MicroLoops™, MicroMeshes™ and MicroGrippers™, and all other standard crystal mounts without epoxy, glue or grease.
Simply insert the mount’s pin into the base, and then push down using our heavy-duty tweezers until the grip is secure.
barcoded goniometer base (y/n)
reusable goniometer base (y/n)
cryovials (y/n)
Use MiTeGen’s Base Holders for secure storage of goniometer bases (caps), pins and assemblies.
Convenient for organizing your MicroMounts™, MicroLoops™, MicroGrippers™ and MicroMeshes™ by size and design, for optimal crystal harvesting and data collection.
| Image | Base Style | Typical Pin Length | Compatible Automated System |
 |
Style B5 | 18 mm | SPINE |
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Style B1 | 19 mm | SAM |
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Style B2 | 11 mm | |
| Style B3 | 19 mm | ||
 |
Style B1A | 18 mm | ALS |
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Style B3S | 18 mm | |
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Style B4 | 18 mm | – |
CryoVials help keep your sample cold during transfer from a dewar to a cold gas stream. They also provide protection against sample damage or loss due to sloshing of liquid nitrogen within a storage dewar.
They have a ring magnet at the open end to attach to a goniometer base (cap), and a magnetic steel ballast at the sealed end to attach to SPINE automounters.
| Products & Ordering |
|
| Magnetic CryoVial | |
| 50 pcs. | CV-50 |
| 100 pcs. | CV-100 |
| 200 pcs. | CV-200 |
Robust and reliable Cryo Tools to handle samples at cryogenic temperatures near 100 K. The tools are compatible with MiTeGen’s 18 mm SPINE loops and mounts, goniometer bases and magnetic CryoVials.
| Products & Ordering | |
| Magnetic Cryo Wand X-CC-101 for SPINE standard bases |
Curved Magnetic Cryo Wand X-CC-102 for SPINE standard bases |
| 18 mm Pin Tong X-CC-103 | Curved CryoVial Tong X-CC-104 |
| CryoVial Tong X-CC-105 |
Mitegen’s ready-to-use assemblies for cryocrystallography consist of your choice of magnetic goniometer bases (caps), and your choice of 18mm/SPINE length crystal mounts/loops, pre-inserted into the bases. They are ready for crystal mounting and data collection.
Each package contains 20 ready-to-use assemblies.
Choose the mount/loop style first and go to the corresponding product page listed below.
Then please choose:
barcoded goniometer base (y/n) reusable goniometer base (y/n) cryovials (y/n)| Dual-Thickness MicroMount Assembly | MicroMesh Assembly | Dual-Thickness MicroLoop Assembly | Dual-Thickness MicroLoop LD Assembly | MicroLoop E Assembly | MicroGripper Assembly |
| Crystal Mount-Base-Vial-Assembly HTA-M2-XX-BY Dual Thickness MicroMount Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly HTA-M3-XX-BY MicroMesh Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly HTA-M5-XX-BY MicroLoop Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly HTA-M5-XXLD-BY MicroLoop LD Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly HTA-M8-XX-BY MicroLoop E Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly HTA-M7-XX-BY MicroGripper Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded bases (By) with cryovials |
| Crystal Mount-Base-Vial-Assembly HTA-M2-XX-BY-R Dual Thickness MicroMount Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded reusable bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly HTA-M3-XX-BY-R MicroMesh Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded reusable bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly HTA-M5-XX-BY-R MicroLoop Assembly with specified aperture size (xx) on 18mm/ SPINE length rods adhered into specified barcoded reusable bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly HTA-M5-XXLD-BY-R MicroLoop LD Assembly with specified aperture size (xx) on 18mm/ SPINE length rods adhered into specified barcoded reusable bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly HTA-M8-XX-BY-R MicroLoop E Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded reusable bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly HTA-M7-XX-BY-R MicroGripper Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded reusable bases (By) with cryovials |
| Crystal Mount-Base-Assembly HTB-M2-XX-BY Dual Thickness MicroMount Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded bases (By) without cryovials | Crystal Mount-Base-Assembly HTB-M3-XX-BY MicroMesh Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded bases (By) without cryovials | Crystal Mount-Base-Assembly HTB-M5-XX-BY MicroLoop Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded bases (By) without cryovials | Crystal Mount-Base-Assembly HTB-M5-XXLD-BY MicroLoop LD Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded bases (By) without cryovials | Crystal Mount-Base-Assembly HTB-M8-XX-BY MicroLoop E Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded bases (By) without cryovials | Crystal Mount-Base-Assembly HTB-M7-XX-BY MicroGripper Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded bases (By) without cryovials |
| Crystal Mount-Base-Assembly HTB-M2-XX-BY-R Dual Thickness MicroMount Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded reusable bases (By) without cryovials | Crystal Mount-Base-Assembly HTB-M3-XX-BY-R MicroMesh Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded reusable bases (By) without cryovials | Crystal Mount-Base-Assembly HTB-M5-XX-BY-R MicroLoop Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded reusable bases (By) without cryovials | Crystal Mount-Base-Assembly HTB-M5-XXLD-BY-R MicroLoop LD Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded reusable bases (By) without cryovials | Crystal Mount-Base-Assembly HTB-M8-XX-BY-R MicroLoop E Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded reusable bases (By) without cryovials | Crystal Mount-Base-Assembly HTB-M7-XX-BY-R MicroGripper Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified barcoded reusable bases (By) without cryovials |
| Crystal Mount-Base-Vial-Assembly A-M2-XX-BY Dual Thickness MicroMount Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly A-M3-XX-BY MicroMesh Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly A-M5-XX-BY MicroLoop Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly A-M5-XXLD-BY MicroLoop LD Assembly with specified aperture size (xx) on 18mm/ SPINE length rods adhered into specified bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly A-M8-XX-BY MicroLoop E Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly A-M7-XX-BY MicroGripper Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified bases (By) with cryovials |
| Crystal Mount-Base-Vial-Assembly A-M2-XX-BY-R Dual Thickness MicroMount Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified reusable bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly A-M3-XX-BY-R MicroMesh Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified reusable bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly A-M5-XX-BY-R MicroLoop Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified reusable bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly A-M5-XXLD-BY-R MicroLoop LD Assembly with specified aperture size (xx) on 18mm/ SPINE length rods adhered into specified reusable bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly A-M8-XX-BY-R MicroLoop E Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified reusable bases (By) with cryovials | Crystal Mount-Base-Vial-Assembly A-M7-XX-BY-R MicroGripper Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified reusable bases (By) with cryovials |
| Crystal Mount-Base-Assembly B-M2-XX-BY Dual Thickness MicroMount Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified bases (By) without cryovials | Crystal Mount-Base-Assembly B-M3-XX-BY MicroMesh Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified bases (By) without cryovials | Crystal Mount-Base-Assembly B-M5-XX-BY MicroLoop Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified bases (By) without cryovials | Crystal Mount-Base-Assembly B-M5-XXLD-BY MicroLoop LD Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified bases (By) without cryovials | Crystal Mount-Base-Assembly B-M8-XX-BY MicroLoop E Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified bases (By) without cryovials | Crystal Mount-Base-Assembly B-M7-XX-BY MicroGripper Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified bases (By) without cryovials |
| Crystal Mount-Base-Assembly B-M2-XX-BY-R Dual Thickness MicroMount Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified reusable bases (By) without cryovials | Crystal Mount-Base-Assembly B-M3-XX-BY-R MicroMesh Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified reusable bases (By) without cryovials | Crystal Mount-Base-Assembly B-M5-XX-BY-R MicroLoop Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified reusable bases (By) without cryovials | Crystal Mount-Base-Assembly B-M5-XXLD-BY-R MicroLoop LD Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified reusable bases (By) without cryovials | Crystal Mount-Base-Assembly B-M8-XX-BY-R MicroLoop E Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified reusable bases (By) without cryovials | Crystal Mount-Base-Assembly B-M7-XX-BY-R MicroGripper Assembly with specified aperture size (xx) on 18mm/SPINE length rods adhered into specified reusable bases (By) without cryovials |
MiTeGen’s patented MicroRT™ capillary system is the answer for room temperature diffraction screening and data collection. Go from a crystal in a drop to a crystal in the X-ray beam at room temperature in 2 minutes with 99% chance of success. Collect room and low temperature data from the same crystal to evaluate your crystal and cryopreservation protocol. And use saturated salt solutions to controllably dehydrate crystals and improve their order.
Each bottle of MicroRT Tubing contains twenty 38 mm (1.5″) long clear polyester tubes sealed at one end, an extra-keen razor blade for cutting the tubes to a desired length, and a tiny tube of grease for lubricating the base.
| Products & Ordering | ||
| MicroRT Tubing Kit RT-T1 contains 20 polyester tubes sealed at one end, a razor blade, and grease |
MicroRT Aligner RTA-1 | Gel Loading Pipette Tips GLPT-1 for filling polyester tubes and capillaries |
LV CryoOil™ is a low viscosity, low surface tension perfluoropolyether oil with extremely low vapor pressure, excellent chemical inertness and excellent thermal stability. It is ideal for cryprotection and for protection against dehydration and oxidation, especially of very small crystals.
The ice rings seen in the diffraction patterns of flash cooled protein crystals arise primarily from crystallization of the aqueous solution surrounding the crystal, not of the internal solvent. Oils can displace and replace this surrounding solution with little risk of damage due to osmotic shock.
However, when mineral oil, Paratone oil and other high viscosity oils are used, the volume of surrounding oil can exceed the crystal volume by a factor of 10 or more, and can contribute excess drag that increases sample motion in a cryostream.
LV CryoOil™ has the lowest viscosity of any available perfluoropolyether oil (1/10 that of Paratone oil and comparable to that of vegetable oil), and a very low surface tension (less than 1/3 that of water.
Consequently, a dip in this oil followed by gentle tapping to shake off excess can yield protective oil films on your crystal of as little as 10 microns thick.
Each vial contains 1.5 ml of oil, enough to protect hundreds of crystals.
NVH Oil is a very high viscosity oil suitable for room and variable-temperature diffraction measurements. Crystal motion during data collection is minimized, even when thick layers are used to prevent dehydration.
This oil is very effective in removing external solvent to prevent ice ring formation during cooling. Move your crystal back and forth in the oil, transfer to fresh oil, and repeat until you no longer see solvent trails and the crystal becomes nearly invisible.
Many protein crystals prepared in this way can be slowly cooled to 100 K without appreciable degradation of diffraction properties, allowing data collection at arbitrary temperatures. Unlike Paratone-N oil, this oil does not form diffraction rings when cooled.
Apiezon N is a Silicon-Free and Halogen-Free cryogenic vacuum grease that is widely recommended and recognized as the grease of choice in cryogenic applications.
A tiny spot of Apiezon N is excellent for affixing small molecules to mitegen mounts, and provides for improved thermal contact. Apiezon N grease can be relied upon to maintain an effective, crack free connection for long periods, even in applications which are subject to frequent thermal cycling.
| Products & Ordering | ||
| LV CryoOil™ LVCO | NVH Oil NVHO-1 | Apiezon N Cryogenic Vacuum Grease APZN-1 |
Crystal Annealing is a promising technique to improve diffraction quality of poorly diffracting protein crystals.
The Cryo Shutter, developed by Dr. Uwe Mueller et al., MX-Lab at BESSY-II, HZB Berlin-Adlershof, is designed for crystal annealing at home sources:
The Cryo Shutter Assembly Kit is available for Cryojet Systems (Oxford Instruments) as well as for Cryostream 700 Systems (Oxford Cryosystems).
Shutter operation requires a compressed air source!
| Products & Ordering | ||
| Cryo Shutter for Cryojet Systems CC-330-19 | Cryo Shutter for Cryojet Systems with limited space CC-330-19LTD | Cryo Shutter for Cryostream 700 Systems CC-330-22 |
The patented VersaPin™ allows you to perform several operations needed to prepare your beamline or home source for diffraction measurements – all with just one tool.
Save time while improving the accuracy of your measurements.
Alignment needle for sample rotation axis alignment:
Scintillator for beam visualization:
Metal Foil for:
| Products & Ordering | |
| VersaPin for Beamlines X-VP-BL01 | VersaPin for Home Sources X-VP-HS01 |
Jena Bioscience distributes MiTeGen’s Crystallography Starter Kits.
| Protein Crystallography Starter Kit™ | Small Molecule Crystallography Starter Kit™ | MicroRT™ Room Temperature Starter Kit | Crystallography Sampler Kit™ |
| MiTeGen’s Crystallography Starter Kit CSK-2 everything to mount and collect X-ray data from your crystals | MiTeGen’s Small Molecule Crystallography Starter Kit SMSK-1 containing 10 reusable goniometer bases (GB-B3S-R) and 10 magnetic CryoVials | MiTeGen’s Room Temperature Starter Kit RTSK-1 everything to get started preparing samples for room temperature screening | Crystal Harvesting Sampler Kit 1 MSK-1 40 tools on 18 mm SPINE length pins |
| MiTeGen’s Small Molecule Crystallography Starter Kit SMSK-2 containing 20 B4 style bases (GB-B4) | Crystal Harvesting Sampler Kit 2 MSK-2 120 tools on 18 mm SPINE length pins |
CryoVials help keep your sample cold during transfer from a dewar to a cold gas stream. They also provide protection against sample damage or loss due to sloshing of liquid nitrogen within a storage dewar.
They have a ring magnet at the open end to attach to a goniometer base (cap), and a magnetic steel ballast at the sealed end to attach to SPINE automounters.
| Products & Ordering |
| Magnetic CryoVial CV-JEN |
The Uni-Puck is a sample pin storage & shipping container compatible with many automated sample mounting systems worldwide. It holds 16 sample bases/pins and consists of two parts: the sample enclosure and the sample base piece.
The Uni-Pucks are stored and shipped in the Puck-Shelved Shipping Cane which fits into the CX100 Dry Shipper.
| Products & Ordering | |
| Uni-Puck Starter Kit X-CC-113 | Uni-Puck X-CC-110 for 16 sample bases/pins |
| Puck-Shelved Shipping Cane X-CC-111 for 7 Uni-Pucks or Cryo-EM Pucks | Bent Cryo Tong X-CC-112 secure transfer of cryo-cooled Uni-Pucks and Cryo-EM Pucks |
| Puck Wand X-CC-114 | Puck Separator Tools X-CC-116 |
| Puck Dewar Loading Tool X-CC-115 | Double Puck Loading Dewar with Lid X-CC-117 |
The SPINE Puck can be loaded with 10 frozen samples mounted on SPINE standard sample holders (Goniometer Base/Cap with CryoVial). Each puck is identified by a unique dot matrix.
The SPINE standard is the sample holder format accepted by most of the sample changers available on MX beamlines in Europe, and elsewhere.
| Products & Ordering | |
| SPINE Puck CC-CSM003-0001A for 10 frozen samples |
Puck Support CC-CSM003-0005A SPINE |
The Puck Support is designed to easily insert / retrieve samples into / from the SPINE Puck.
The High Capacity (HC) Cryogenic Refrigerators from Worthington Industries are designed for long-term storage of biological material at liquid nitrogen temperature. Temperatures generally range between –196°C at the liquid surface, and –190°C at the canister top. Different models offer a variety of choices between sample storage capacity and holding time, while offering easier access to stored materials due to larger neck openings.
HC models feature:
| Products & Ordering | |
| HC34 High-Capacity Refrigerator X-HC34 | VHC35 High-Capacity Refrigerator X-VHC35 |
| HC35 High-Capacity Refrigerator X-HC35 | Roller Base X-HCRB for HC34, HC35 & VHC35 |
| Model | HC34 | HC35 | VHC35 |
| Static Holding Days | 200 | 130 | 130 |
| Working Time Days | 125 | 81 | 81 |
| Evaporation Rate (liters/day) | 0,17 | 0,27 | 0,27 |
| Liquid Nitrogen Capacity (liters) | 34 | 35 | 35 |
| Weight Empty (kg) | 16,1 | 17,7 | 17,2 |
| Weight Full (kg) | 43,6 | 46 | 45,5 |
| Neck Diameter (mm) | 91 | 119 | 119 |
| Overall Height (mm) | 668 | 681 | 681 |
| Overall Diameter (mm) | 478 | 478 | 478 |
| Number of Canisters | 6 | 10 | 6 |
| Canister Dimensions (mm) | 70 x 279 | 67 x 279 | 94 x 279 |
Cryo Express (CX) Dry Shippers from Worthington Industries are designed to safely transport a variety of materials at cryogenic temperatures. The unique absorbent material prevents a liquid spill if the unit is tipped over. Storage temperature inside the shipping cavity remains at approximately -190°C until the liquid nitrogen evaporates from the absorbent material.
The replaceable absorbent material enables easy cleaning of the CXR100 dry shipper.
Technical Specifications for CX and CXR Dry Shippers
| Products & Ordering | ||
| Cryo Express Dry Shipper & Alu Shipping Case CC-CX100ASC | Cryo Express Dry Shipper CC-CXR100 with Replaceable Absorbent Material | Plastic Shipping Case for CX100 and CXR100 X-CX10SC |
| Cryo Express Dry Shipper CC-CX100 | Alu Shipping Case for CX100 and CXR100 CC-CX10-8C00K | Replaceable Absorbent Material for CXR100 CC-CXR100-9C30 |
The Standard Foam Dewar can hold 800 ml of liquid nitrogen. It has been designed to replace large glass dewars, because the foam has superior durability, safety, insulating properties.
The standard vessel shape is circular, with a protruding handle. Each dewar comes with a matching foam lid to insulate the contents from ambient air.
Dimensions of the cylindrical cavity in this vessel are 15 cm in diameter by 7 cm in depth.
The Small Foam Dewar has the same basic shape and features as the Standard Foam Dewar but a smaller diameter cavity . Dimensions of the cylindrical cavity are 11.5 cm in diameter by 7 cm in depth, easily holding 500 ml of cryogenic liquid.
The Large Foam Dewar is a slightly bigger version of the popular standard vessel. Dimensions of the cylindrical cavity in this vessel are 16 cm in diameter by 9.5 cm in depth, so that it easily holds 1400 ml of liquid nitrogen.
The Tall Foam Dewar was initially developed for short term storage of canes of protein crystallography samples. The tall vessel, like the standard vessel, offers excellent durability and safety. Its insulating properties are comparable to those of conventional stainless steel and glass Dewars, at a fraction of the cost.
This vessel has a 9 cm diameter cylindrical cavity, 32 cm deep, which gives it a capacity of 1800 ml liquid nitrogen.
The Mini Foam Dewar is our smallest foam dewar. In the photo to the right, it is the smaller of the two vessels shown. The cylindrical cavity in this vessel is 5 cm in diameter by 8.9 cm deep, so that it easily holds 130 ml and a maximum volume of 175 ml of liquid nitrogen. Perfect for applications that require a small quantity of cryogenic liquid.
| Products & Ordering | ||
| Small Foam Dewar CC-FD-500 500 ml capacity, 11.5 cm diameter, 7 cm deep |
Standard Foam Dewar CC-FD-800 800 ml capacity, 15 cm diameter, 7 cm deep |
Large Foam Dewar CC-FD-1400 1400 ml capacity, 16 cm diameter, 9.5 cm deep |
| Tall Foam Dewar CC-TD-1800 1800 ml capacity, 9 cm diameter, 32 cm deep |
Mini Foam Dewar CC-FD-130 130 ml capacity, 5 cm diameter, 8.9 cm deep |
CryoSleeves™ are clear plastic sleeves designed to enclose CryoCane™ holders for extra security during handling and storage. They allow quick location of empty spaces in the cane and easy identification of a particular vial or vials without removing the sleeve.
CryoSleeves™ are a direct replacement for cardboard sleeves and will not become brittle while frozen.
| Products & Ordering |
| CryoSleeve™ CC-305 |
Cryoware labels are specifically designed for use at ultra-low temperatures. The cloth labels adhere to plastic and cardboard cryogenic storage boxes and will not peel or shrink. They accept ballpoint pens, but they are not printer compatible. Ten sheets of labels with twenty labels per sheet will be supplied.
Base Holders for secure and convenient storage of goniometer bases (caps), pins and assemblies:
Base Holders are perfectly suited for Cleaning MicroMounts™, MicroLoops™, MicroMeshes™, MicroGrippers™ and MicroTools™. Please find detailed information in the Cleaning Instructions below or simply order the Cleaning Kit, #BHCK-1.
| Products & Ordering |
| Base Holders GB-BH |
| Base Holder and Cleaning Kit BHCK-1 |
| Products & Ordering |
| Goniometer Head Adapter GHA-1 |
| Products & Ordering |
| Serrated End Tweezers TW-1 Heavy duty finely crafted tweezers |
High quality Pin Cutters provide accurate, burr-free cutting of the hard-temper stainless steel pins used in Dual-Thickness MicroMounts™, Dual-Thickness MicroLoops™, MicroMeshes™, etc.
| Products & Ordering |
| Pin Cutters PC-102 |
The Phasing Section contains carefully selected heavy-atom kits that are suitable for single/multiple isomorphous replacement (SIR and MIR) experiments and anomalous dispersion (SAD and MAD) experiments. Furthermore, there are many nucleotide analogs – designed to introduce heavy atoms in ATP/GTP-binding enzymes.
Talk held at HEC 16, September 28, 2013
| Products & Ordering |
| Tantalum Cluster Derivatization Kit PK-103 |
The very electron-rich Tantalum Bromide Cluster induces significant changes in crystal diffraction required for convenient phase calculation in single and multiple isomorphous replacement (SIR and MIR) experiments and in anomalous dispersion (SAD and MAD) experiments.
The two present anomalous scatterers Ta and Br are useful for determining the cluster orientation for low resolution datasets.
Tantalum Bromide Clusters have been successfully employed in several structural studies because of their high electron-density, solubility in aqueous solutions and stability over a wide pH range.
Heavy atom derivatization of biological macromolecules for isomorphous and/or anomalous phasing methods.
Experimental Tungsten (W) Phasing – either by SAD/MAD or MIR experiments – has become increasingly popular due to the high electron-density and good solubility in aqueous solutions of Polyoxotungstate Clusters.
The Tungstate Cluster Kits consist of 6 ready-to-use aliquots of Phosphotungstate, Metatungstate or Paratungstate salts, respectively. All Tungsten clusters contain 12 Tungsten metal centers bridged by Oxygen atoms, but differ in their resulting negative charge (3-, 6- and 10-, respectively).
| Products & Ordering | |
| JBS Phosphotungstate Cluster Kit PK-105 | JBS Paratungstate Cluster Kit PK-107 |
| JBS Metatungstate Cluster Kit PK-106 | JBS Tungstate Cluster Kit PK-108 contains 3 different clusters |
| Products & Ordering |
| JBS Magic Triangle PK-104 |
JBS Magic Triangle is a phasing kit developed in co-operation with Tobias Beck in the research group of Prof. George M. Sheldrick, Georg-August University Göttingen.
The “Magic Triangle” I3C consists of three iodine atoms forming an equilateral triangle with a side length of 6.0 Å that can readily be identified in the electron density map.
It has been demonstrated for heavy-atom derivatization of macromolecules, and experimental phases have been derived using single-wavelength anomalous dispersion (SAD) or single isomorphous replacement plus anomalous scattering (SIRAS) methods.
Lanthanide derivatives of protein crystals are obtained either by soaking or co-crystallization. They can be used as strong anomalous scatterers due to the lanthanide LIII absorption edge.
| Products & Ordering | ||
| LuXo4-01-P X-PK-201 Crystallophore’s Lanthanide Phasing Compound | TbXo4-02-P X-PK-202 Crystallophore’s Lanthanide Phasing Compound | Eu-DOTA X-PK-203 Lanthanide Phasing Compound |
| Eu-(DPA)3 X-PK-204 Lanthanide Phasing Compound | Lu-DO3A X-PK-205 Lanthanide Phasing Compound | Lu-HPDO3A X-PK-206 Lanthanide Phasing Compound |
The most simple method currently used for solution of the macromolecular phase problem, single wavelength anomalous dispersion (SAD), still involves the incorporation of heavy atoms into protein crystals. After crystallization, finding such derivatives is the second major bottleneck in the determination of the 3D structure of bio-macromolecules.
Most labeling procedures focus on the protein itself in a “trial and error” fashion.
Mercurated C/UTP nucleotides provide an alternative method that allows rational incorporation of heavy atoms into a large number of physiologically relevant enzymes like DNA polymerases and nucleotidyl transferases. Mercury displays a strong anomalous signal at its LIII absorption edge suitable for SAD and MAD experiments.
| Products & Ordering | |
| 5-AcOHg-dCTP NU-1149 | 5-AcOHg-dUTP NU-910 |
The most simple method currently used for solution of the macromolecular phase problem, single wavelength anomalous dispersion (SAD), still involves the incorporation of heavy atoms into protein crystals. After crystallization, finding such derivatives is the second major bottleneck in the determination of the 3D structure of bio-macromolecules.
Most labeling procedures focus on the protein itself in a “trial and error” fashion.
Selenium-containing nucleotides provide an alternative method that allows rational incorporation of the heavy atom into a large number of physiologically relevant ATP-binding enzymes like kinases, motor proteins and chaperones. Selenium derivative crystals are well suitable for SAD and MAD experiments. Please note that it is recommended one selenium atom per 50 amino acids for weakly diffraction crystals.
| Products & Ordering |
| 2’MeSe-ATP NU-928 |
Cryo-electron microscopy (Cryo-EM) is a technique that uses accelerated electrons as illumination source for biological samples. To minimize radiation damage, the sample is kept at cryogenic temperatures and the electron dose has to be low – resulting in noisy images. However, the enormous progress in hardware development and image processing in the last decade has made the technique available to solve near-atomic-resolution protein structures. And the technological progress is ongoing: With even better instruments and software the size and resolution limit will be pushed further down[1].
Today, Cryo-EM does not replace but rather complements X-ray crystallography as structural biology technique[2,3].
The surfactant Amphipol A8-35 stabilizes membrane proteins in a detergent-free aqueous solution and is therefore a useful additive for sample preparation in Cryo-EM.
[1] Glaeser (2016) How good can cryo-EM become? Nature Methods 13:28.
[2] Beniac et al. (2017) Structure of the Ebola virus glycoprotein spike within the virion envelope at 11 Å resolution. Sci. Rep. DOI: 10.1038/srep46374.
[3] Lokareddy et al. (2017) Portal protein functions akin to a DNA-sensor that couples genome-packaging to icosahedral capsid maturation. Nat. Commun. DOI: 10.1038/ncomms14310.
Single particle electron cryo-microscopy (cryo-EM) is a powerful technique to determine the structures of protein complexes down to atomic resolution. The sample in solution is flash-frozen in liquid ethane, forming a thin layer of vitreous ice, in which the sample particles are ideally evenly distributed in random orientation far enough from the air-water interface (pictured below).
However, protein sample vitrification for cryo-EM is a major bottleneck. Only the combination of choosing the right grid type, vitrification conditions, protein concentration and additives enables high quality data acquisition in cryo-EM.
The Cryo-EM V-Kit is a Vitrification Starter Kit that offers both a selection of surfactants which have been successfully applied in cryo-EM sample preparation and a selection of Quantifoil Holey Carbon Films to facilitate the search for the optimal vitrification condition for both soluble and membrane proteins.
Schematic cross section of a grid hole with ideally distributed single particles in random orientation.
| Products & Ordering |
| Cryo-EM V-Kit X-CEM-301 Vitrification Starter Kit |
Quantifoil® is a holey carbon film with a thickness of about 12 nm, that is applied on a standard copper or gold electron microscopy grid and provides an ideal support for biological samples in cryo-EM techniques[1-8].
The supporting mesh (copper or gold) is available with distinct numbers. Higher mesh numbers (400) indicate closely spaced bars and provide higher stability, whereas lower numbers (200) provide larger free faces.
The Quantifoil® carbon film has circular holes of defined size and interspace, e.g. R 2/1 (pictured) has holes of 2 µm diameter with an interspace of 1 µm in both dimensions. Higher magnifications usually require smaller holes and vice versa.
You have the following options to choose from:
Quantifoil® film
Supporting mesh material
Supporting mesh number
| Products & Ordering | |||
| Quantifoil™ R 0.6/1 on 300 copper mesh X-100-CU300 | Quantifoil™ R 1.2/1.3 on 300 copper mesh X-101-CU300 | Quantifoil™ R 2/1 on 300 copper mesh X-102-Cu300 | Quantifoil™ R 2/2 on 300 copper mesh X-103-Cu300 |
| Quantifoil™ R 0.6/1 on 300 gold mesh X-100-AU300 | Quantifoil™ R 1.2/1.3 on 300 gold mesh X-101-AU300 | Quantifoil™ R 2/1 on 300 gold mesh X-102-Au300 | Quantifoil™ R 2/2 on 300 gold mesh X-103-Au300 |
| Quantifoil™ R 1/4 on 200 copper mesh X-105-CU200 | Quantifoil™ R 1.2/1.3 on 400 copper mesh X-101-Cu400 | Quantifoil™ R 2/1 on 400 copper mesh X-102-Cu400 | Quantifoil™ R 2/2 on 400 copper mesh X-103-Cu400 |
| Quantifoil™ R 1/4 on 200 gold mesh X-105-AU200 | Quantifoil™ R 1.2/1.3 on 400 gold mesh X-101-Au400 | Quantifoil™ R 2/1 on 400 gold mesh X-102-Au400 | Quantifoil™ R 2/2 on 400 gold mesh X-103-Au400 |
| Quantifoil™ R 1.2/1.3 on 200 copper mesh X-101-CU200 | Quantifoil™ R 2/1 on 200 copper mesh X-102-Cu200 | Quantifoil™ R 2/2 on 200 copper mesh X-103-Cu200 | Quantifoil™ R 3.5/1 on 200 copper mesh X-104-Cu200 |
| Quantifoil™ R 1.2/1.3 on 200 gold mesh X-101-AU200 | Quantifoil™ R 2/1 on 200 gold mesh X-102-Au200 | Quantifoil™ R 2/2 on 200 gold mesh X-103-Au200 |
[1] Lee et al. (2019) Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation. Cell Reports 26:29.
[2] Azubel et al. (2019) FGF21 trafficking in intact human cells revealed by cryo-electron tomography with gold nanoparticles. eLife DOI:10.7554/eLife.43146.
[3] Zhao et al. (2018) Structure and mechanogating mechanism of the Piezo1 channel. Nature 554:487.
[4] Wijnands et al. (2018) Controlling protein activity by dynamic recruitmenton a supramolecular polymer platform. Nat. Commun. 9:65.
[5] Ke et al. (2018) Promotion of virus assembly and organization by the measles virus matrix protein. Nat. Commun. 9:1736.
[6] Zhang et al. (2018) Molecular structure of the ATP-bound, phosphorylated human CFTR. PNAS 115:12757.
[7] Park et al. (2017) Structure of a CLC chloride ion channel by cryo-electron microscopy. Nature 541:500.
[8] Ekiert et al. (2017) Architectures of Lipid Transport Systems for the Bacterial Outer Membrane. Cell 169:273.
Quantifoil® is a holey carbon film with a special geometry and a thickness of about 12 nm, that is applied on a standard copper electron microscopy grid and provides an ideal support for biological samples in cryo-EM techniques[1-8]. Higher mesh numbers (300) indicate closely spaced bars and provide higher stability, whereas lower numbers (200) provide larger free faces. The Quantifoil® carbon film has circular holes of defined size and interspace, e.g. R 2/1 (pictured) has holes of 2 µm diameter with an interspace of 1 µm in both dimensions.
The C2 versions on this page provide an additional 2 nm continuous carbon layer on top.
| Products & Ordering | ||
| Quantifoil™ R 1.2/1.3 plus C2 on 200 copper mesh X-101-Cu200C2 | Quantifoil™ R 2/1 plus C2 on 200 copper mesh X-102-Cu200C2 | Quantifoil™ R 2/2 plus C2 on 300 copper mesh X-103-CU300C2 |
| Quantifoil™ R 1.2/1.3 plus C2 on 300 copper mesh X-101-CU300C2 | Quantifoil™ R 2/1 plus C2 on 300 copper mesh X-102-Cu300C2 |
[1] Lee et al. (2019) Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation. Cell Reports 26:29.
[2] Azubel et al. (2019) FGF21 trafficking in intact human cells revealed by cryo-electron tomography with gold nanoparticles. eLife DOI:10.7554/eLife.43146.
[3] Zhao et al. (2018) Structure and mechanogating mechanism of the Piezo1 channel. Nature 554:487.
[4] Wijnands et al. (2018) Controlling protein activity by dynamic recruitmenton a supramolecular polymer platform. Nat. Commun. 9:65.
[5] Ke et al. (2018) Promotion of virus assembly and organization by the measles virus matrix protein. Nat. Commun. 9:1736.
[6] Zhang et al. (2018) Molecular structure of the ATP-bound, phosphorylated human CFTR. PNAS 115:12757.
[7] Park et al. (2017) Structure of a CLC chloride ion channel by cryo-electron microscopy. Nature 541:500.
[8] Ekiert et al. (2017) Architectures of Lipid Transport Systems for the Bacterial Outer Membrane. Cell 169:273.
UltrAuFoil® is a holey gold film with a thickness of about 500 Å, that provides an ultrastable gold support for for biological samples in cryo-EM techniques. The movement of frozen specimens during imaging will be significantly reduced leading to better image contrast and finally to better 3D reconstructions with less data[1].
| Products & Ordering | ||
| UltrAuFoil® R 0.6/1 on 300 gold mesh X-200-Au300 | UltrAuFoil® R 1.2/1.3 on 300 gold mesh X-201-Au300 | UltrAuFoil® R 2/2 on 200 gold mesh X-203-Au200 |
[1] Russo et al. (2014) Ultrastable gold substrates for electron cryomicroscopy. Science 346:1377.
The Carbon Support Film is a continuous carbon film with a thickness of 10 nm, typically used for negative staining of biological samples in cryo-em techniques.
Quantifoil Multi Holes offer a pattern of various hole sizes, shapes and arrangements and are typically used in cryo-tomography (cryo-ET) or cryo-electron microscopy (cryo-EM) techniques.
Lacey Carbon Films offer a lacey mesh structure with a high percentage of open area. The hole sizes vary significantly and the bars are extremely thin.
| Products & Ordering | ||
| Carbon Support Film on 300 copper mesh X-150-CU300 | Quantifoil™ Multi Holes on 200 copper mesh X-160-CU200 | Lacey Carbon Film on 400 copper mesh X-170-CU400 |
C-flat™ is an ultra-flat, holey carbon film with a thickness of about 20 nm supported by a standard transmission electron microscopy (TEM) grid. The precise patent pending technology by which C-flat™ is manufactured eliminates artifacts such as excess carbon and edges around holes. The ultra-flat surface results in better particle dispersion and more uniform ice thickness. Manufactured without plastics, C-flat™ grids are clean upon arrival and the user has no residue to contend with. The C-flat™ carbon film has circular holes of defined size and interspace, e.g. CF 2/2 (pictured) has holes of 2 µm diameter with an interspace of 2 µm in both dimensions.
You have the following options to choose from:
C-flat™ film
Supporting TEM grid material
Supporting TEM grid mesh size
Looking for gold? Check out the Au-flat™ Holey Gold Films!
| Products & Ordering | |
| C-flat™ 1.2/1.3 on 200 copper mesh X-301-CU200 | C-flat™ 2/1 on 300 gold mesh X-302-AU300 |
| C-flat™ 1.2/1.3 on 200 gold mesh X-301-AU200 | C-flat™ 2/1 on 400 copper mesh X-302-CU400 |
| C-flat™ 1.2/1.3 on 300 copper mesh X-301-CU300 | C-flat™ 2/1 on 400 gold mesh X-302-AU400 |
| C-flat™ 1.2/1.3 on 300 gold mesh X-301-AU300 | C-flat™ 2/2 on 200 copper mesh X-303-CU200 |
| C-flat™ 1.2/1.3 on 400 copper mesh X-301-CU400 | C-flat™ 2/2 on 200 gold mesh X-303-AU200 |
| C-flat™ 1.2/1.3 on 400 gold mesh X-301-AU400 | C-flat™ 2/2 on 300 copper mesh X-303-CU300 |
| C-flat™ 2/1 on 200 copper mesh X-302-CU200 | C-flat™ 2/2 on 300 gold mesh X-303-AU300 |
| C-flat™ 2/1 on 200 gold mesh X-302-AU200 | C-flat™ 2/2 on 400 copper mesh X-303-CU400 |
| C-flat™ 2/1 on 300 copper mesh X-302-CU300 | C-flat™ 2/2 on 400 gold mesh X-303-AU400 |
Au-flat™ is an ultrastable holey gold alloy film (80% Au and 20% Pd) with a thickness of about 45 nm supported by a transmission electron microscopy (TEM) gold grid. It’s a derivative of the patented C-flat™ holey carbon films.
| Products & Ordering | ||
| Au-flat™ 0.6/1.0 on 300 gold mesh X-400-AU300 | Au-flat™ 1.2/1.3 on 300 gold mesh X-401-AU300 | Au-flat™ 2/2 on 200 gold mesh X-403-AU200 |
Amphipols are short amphipatic polymers that are specifically designed to stabilize membrane proteins in aqueous solutions.
Due to their dense distribution of hydrophobic chains they tightly bind to transmembrane surfaces of membrane proteins and cover it with a thin interfacial layer of surfactant[1]. The resulting small hydrophilic complexes have several advantages over usually much larger protein detergent complexes, such as stability and functionality of the membrane protein.
Amphipol A8-35 is successfully applied as stabilizing agent in Cryo-EM[2-5] and X-ray crystallography[6].
| Products & Ordering |
| Amphipol A8-35 X-A835 |
| Products & Ordering |
| Amphipol A8-35 X-A835 |
[1] Zoonens et al. (2014) Amphipols for Each Season. J Membrane Biol 247:759.
[2] Chen et al. (2016) Structure of the STRA6 receptor for retinol uptake. Science 353:887.
[3] Zubcevic et al. (2016) Cryo-Electron Microscopy of the Trpv2 Ion Channel. Nat Struct Mol Biol 23:180.
[4] Bai et al. (2015) Sampling the conformational space of the catalytic subunit of human gamma-secretase. DOI 10.7554/eLife.11182.
[5] Althoff et al. (2011) Arrangement of electron transport chain components in bovine mitochondrial supercomplex I1III2IV1. EMBO J 30:4652.
[6] Polovinkin et al. (2014) High-Resolution Structure of a Membrane Protein Transferred from Amphipol to a Lipidic Mesophase. J Membrane Biol 247:997.
Cryo Express (CX) Dry Shippers from Worthington Industries are designed to safely transport a variety of materials at cryogenic temperatures. The unique absorbent material prevents a liquid spill if the unit is tipped over. Storage temperature inside the shipping cavity remains at approximately -190°C until the liquid nitrogen evaporates from the absorbent material.
The replaceable absorbent material enables easy cleaning of the CXR100 dry shipper.
Technical Specifications for CX and CXR Dry Shippers
| Products & Ordering | |
| Cryo Express Dry Shipper & Alu Shipping Case CC-CX100ASC | Alu Shipping Case for CX100 and CXR100 CC-CX10-8C00K |
| Cryo Express Dry Shipper CC-CX100 | Plastic Shipping Case for CX100 and CXR100 X-CX10SC |
| Cryo Express Dry Shipper CC-CXR100 with Replaceable Absorbent Material | Replaceable Absorbent Material for CXR100 CC-CXR100-9C30 |
The High Capacity (HC) Cryogenic Refrigerators from Worthington Industries are designed for long-term storage of biological material at liquid nitrogen temperature. Temperatures generally range between –196°C at the liquid surface, and –190°C at the canister top. Different models offer a variety of choices between sample storage capacity and holding time, while offering easier access to stored materials due to larger neck openings.
HC models feature:
| Products & Ordering | |
| HC34 High-Capacity Refrigerator X-HC34 | VHC35 High-Capacity Refrigerator X-VHC35 |
| HC35 High-Capacity Refrigerator X-HC35 | Roller Base X-HCRB for HC34, HC35 & VHC35 |
| Model | HC34 | HC35 | VHC35 |
| Static Holding Days | 200 | 130 | 130 |
| Working Time Days | 125 | 81 | 81 |
| Evaporation Rate (liters/day) | 0,17 | 0,27 | 0,27 |
| Liquid Nitrogen Capacity (liters) | 34 | 35 | 35 |
| Weight Empty (kg) | 16,1 | 17,7 | 17,2 |
| Weight Full (kg) | 43,6 | 46 | 45,5 |
| Neck Diameter (mm) | 91 | 119 | 119 |
| Overall Height (mm) | 668 | 681 | 681 |
| Overall Diameter (mm) | 478 | 478 | 478 |
| Number of Canisters | 6 | 10 | 6 |
| Canister Dimensions (mm) | 70 x 279 | 67 x 279 | 94 x 279 |
The 2nd generation of MiTeGen’s Cryo-EM pucks has enhanced features, which make them superior to other cryo-EM pucks on the market. They contain magnets in the bottom of the pucks for strong puck retention but easy removal from the shelves of the Cryo-EM Puck Shipping and Storage Canes. A front grabbing tong location for Cryo-EM Puck Grasping Tongs makes puck handling even more secure. Custom 2D barcoding and puck serialization allow advanced sample tracking, a multi-color option completes sample organization and tracking. Each puck has 12 numbered well locations with easy-access tweezer notches for Cryo-EM Grid Boxes.
| Products & Ordering | |
| Cryo-EM Puck Gen 2.0 X-CEMG2 | Cryo-EM Puck Shipping Cane for CX100 X-CEM-204 for 8 Cryo-EM Pucks |
| Cryo-EM Puck Grasping Tongs X-CEM-GT | Cryo-EM Grid Boxes X-CEM-201 |
| Cryo-EM Puck Storage Cane for HC34 & VHC35 X-CEM-202 for 10 Cryo-EM Pucks | Flat Tip Tweezers X-TW-2 |
| Cryo-EM Puck Storage Cane for HC35 X-CEM-203 for 10 Cryo-EM Pucks | Cryo-EM Puck Basic Starter Kit X-CEMG2-BLSK |
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