jena–Protein Crystallization Starter Kit

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Crystallography & Cryo-EM
  • Get started
    • Protein Crystallization Starter Kit
    • JBS Crystallization Freshman Kit – Junior
    • Crystallization of Model Proteins
    • Crystal Handling Kit
  • Screening
  • Screening Membrane Proteins
  • Optimization
  • Data Collection
  • Phasing
  • Cryo-EM

You are here: Crystallography & Cryo-EM | Get started | Protein Crystallization Starter Kit
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Protein Crystallization Starter Kit

Protein Crystallization Starter Kit

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:

  • Growing Lysozyme crystals using the hanging drop method, demonstrating the dependence of crystal formation and crystal growth on salt concentration and buffer pH
  • Growing Lysozyme crystals within minutes using the batch crystallization method

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

Proteinkristallisation Starter Kit – Deutsche Version CS-401DE
 

Protein Crystallization Starter Kit – English Version CS-401EN
 

Kit d’ Initiation à la Cristallisation des Protéines – Version Française CS-401FR
 

Kit de Iniciación a la Cristalización de Proteínas – Versión Española CS-401ES
 

Kit de Iniciação para a Cristalização Proteica – Versão Portuguesa CS-401PT
 

If you are a school or any other educational organization, please contact us for educational discounts!

jena–JBS Crystallization Freshman Kit – Junior

上海金畔生物代理jena品牌蛋白结晶试剂耗材工具等,我们将竭诚为您服务,欢迎访问jena官网或者咨询我们获取更多相关jena品牌产品信息。

Crystallography & Cryo-EM
  • Get started
    • Protein Crystallization Starter Kit
    • JBS Crystallization Freshman Kit – Junior
    • Crystallization of Model Proteins
    • Crystal Handling Kit
  • Screening
  • Screening Membrane Proteins
  • Optimization
  • Data Collection
  • Phasing
  • Cryo-EM

You are here: Crystallography & Cryo-EM | Get started | JBS Crystallization Freshman Kit – Junior
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JBS Crystallization Freshman Kit – Junior

Application

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.

Kit Contents

JBS Crystallization Freshman Kit - Junior

The JBS Crystallization Freshman Kit – Junior contains the required material to crystallize your protein under investigation using the “Hanging Drop Method”:

  • 4 Crystalgen SuperClear™ Plates, pregreased (CPL-132)
  • 100 Thick Circular Cover Slides, siliconized (CSL-107)
  • 96 unique screening conditions, 1.7 ml each: JBScreen JCSG++ HTS (CS-206L)
  • a detailed User Guide

How does one manage to grow crystals from such complicated molecules like proteins?

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.

 
JBS Crystallization Freshman Kit - JuniorBackground Information
JBS Crystallization Freshman Kit - JuniorScoring Sheet

Products & Ordering

JBS Crystallization Freshman Kit – Junior CSK-101
Get a head start crystallizing your protein

JBS Crystallization Freshman Kit - JuniorBackground Information
JBS Crystallization Freshman Kit - JuniorScoring Sheet

jena–Crystallization of Model Proteins

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Crystallography & Cryo-EM
  • Get started
    • Protein Crystallization Starter Kit
    • JBS Crystallization Freshman Kit – Junior
    • Crystallization of Model Proteins
    • Crystal Handling Kit
  • Screening
  • Screening Membrane Proteins
  • Optimization
  • Data Collection
  • Phasing
  • Cryo-EM

You are here: Crystallography & Cryo-EM | Get started | Crystallization of Model Proteins
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Crystallization of Model Proteins

Crystallization of Model Proteins

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:

  • Lysozyme (Chicken egg white)
  • Proteinase K (Tritirachium album)

Products & Ordering

Lysozyme – Solution CO-401
Crystallization grade model protein

Proteinase K – lyophilised CO-404
Crystallization grade model protein

jena–Crystal Handling Kit

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Crystallography & Cryo-EM
  • Get started
    • Protein Crystallization Starter Kit
    • JBS Crystallization Freshman Kit – Junior
    • Crystallization of Model Proteins
    • Crystal Handling Kit
  • Screening
  • Screening Membrane Proteins
  • Optimization
  • Data Collection
  • Phasing
  • Cryo-EM

You are here: Crystallography & Cryo-EM | Get started | Crystal Handling Kit
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Crystal Handling Kit

Crystal Handling Kit

The Crystal Handling Kit will help you to acquire skills in protein crystallization, crystal mounting and data collection.

Each kit contains:

  • 3 proteins, i.e. Lysozyme, Xylanase and Proteinase K
  • optimized solubilization and crystallization buffers for each protein
  • MicroMounts™ and Goniometer Bases, as well as
  • a user manual with instructions for protein crystallization using the hanging-drop vapor diffusion method and crystal mounting using MiTeGen’s MicroMounts™

Products & Ordering

Crystal Handling Kit CO-150
 

jena–Fragment Screen

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Crystallography & Cryo-EM
  • Get started
  • Screening
    • Fragment Screen
    • XP Screens
    • Crystal Screens
    • Thermofluor Screens
    • Detergent Screens
    • Additive Screens
    • Buffer Screens
    • Solubility & Stability Screens
    • Plates & Accessories
    • Oils & Dyes
  • Screening Membrane Proteins
  • Optimization
  • Data Collection
  • Phasing
  • Cryo-EM

You are here: Crystallography & Cryo-EM | Screening | Fragment Screen
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Fragment Screen

Fragment Screen

A major challenge in drug discovery is the identification of chemical moieties that specifically interact with a particular protein target. Traditionally, this was addressed by High Throughput Screening (HTS) however, recently “Fragment Screening” has become increasingly popular. In a Fragment Screen a set of small molecules (“fragments”), typically with MW < 300 Da and with low affinities, are evaluated for specific interaction with the target. Crystallography/X-ray diffraction shows not only whether a fragment binds to the protein but also where and how the binding occurs and is therefore the favored screening method. Hit-fragments are subsequently chemically modified in several optimization/screening cycles until a high affinity lead structure is obtained. Since such a fragmented approach allows screening of broader chemical space compared to large, distinct libraries, the hit rates of Fragment Screens are believed to be 10-1000x higher than those in traditional HTS[5].
The Frag Xtal Screen offers an easy entry to fragment-based lead discovery (FBLD) by crystallographic screening:

  • 96 fragments
  • High fragment solubility allows high soaking concentrations (> 90 mM; may depend on soaking conditions)
  • In-house tests with high crystallographic hit rates
  • Validated X-Ray hits for diverse target classes in the PDB
  • Diverse and representative fragment library for large chemical space
  • Straight-forward follow-up compounds available
 
Fragment ScreenFlyer Frag Xtal Screen

Products & Ordering

Frag Xtal Screen X-FS-101
Fragment Screen for Crystallographic Screening

References / Recommended Literature

[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.

  • 96 fragments
  • High fragment solubility allows high soaking concentrations (> 90 mM; may depend on soaking conditions)
  • In-house tests with high crystallographic hit rates
  • Validated X-Ray hits for diverse target classes in the PDB
  • Diverse and representative fragment library for large chemical space
  • Straight-forward follow-up compounds available
Fragment ScreenFlyer Frag Xtal Screen

jena–XP Screens – Intelligent Crystal Screens

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Crystallography & Cryo-EM
  • Get started
  • Screening
    • Fragment Screen
    • XP Screens
    • Crystal Screens
    • Thermofluor Screens
    • Detergent Screens
    • Additive Screens
    • Buffer Screens
    • Solubility & Stability Screens
    • Plates & Accessories
    • Oils & Dyes
  • Screening Membrane Proteins
  • Optimization
  • Data Collection
  • Phasing
  • Cryo-EM

You are here: Crystallography & Cryo-EM | Screening | XP Screens
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XP Screens – Intelligent Crystal Screens

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.

TEW…

  • is highly soluble in aqueous solutions and stable over a wide pH range
  • has a high negative charge that links positively charged protein surface regions, the electrostatic spacer effect prevents steric interference between protein molecules
  • provides a valuable anomalous signal for phasing
  • can act as linker in various orientations (pictured below) and even structurally adapt to fit into the protein molecule[3]
  • is able to induce heterogeneous crystallization, e.g. two different protein forms in one single crystal[6]
XP Screens - Intelligent Crystal Screens

Protein-protein bridging by TEW in different orientations
Image from [1], used by courtesy of Prof. Annette Rompel, University of Vienna, Austria

 
XP Screens - Intelligent Crystal Screens Flyer XP Screens

Products & Ordering

XP Up Screen CS-351
Crystallization Screen for high TEW concentrations

XP Screen CS-350
Crystallization Screen for improved Crystal Quality and Phasing

Anderson-Evans polyoxotungstate X-TEW
 

Selected Literature Citations of XP Screen

  • Sobala et al. (2020) Structure of human endo-α-1,2-mannosidase (MANEA), an antiviral host-glycosylation target. PNAS 117 (47):29595.
  • Ames et al. (2020) Identifying a Molecular Mechanism That Imparts Species-Specific Toxicity to YoeB Toxins. Front Microbiol 11:959.

References / Recommended Literature

[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.

  • is highly soluble in aqueous solutions and stable over a wide pH range
  • has a high negative charge that links positively charged protein surface regions, the electrostatic spacer effect prevents steric interference between protein molecules
  • provides a valuable anomalous signal for phasing
  • can act as linker in various orientations (pictured below) and even structurally adapt to fit into the protein molecule[3]
  • is able to induce heterogeneous crystallization, e.g. two different protein forms in one single crystal[6]
XP Screens - Intelligent Crystal Screens Flyer XP Screens
  • Sobala et al. (2020) Structure of human endo-α-1,2-mannosidase (MANEA), an antiviral host-glycosylation target. PNAS 117 (47):29595.
  • Ames et al. (2020) Identifying a Molecular Mechanism That Imparts Species-Specific Toxicity to YoeB Toxins. Front Microbiol 11:959.

jena–Crystal Screens

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Crystallography & Cryo-EM
  • Get started
  • Screening
    • Fragment Screen
    • XP Screens
    • Crystal Screens
      • JBScreen Classic
      • JBScreen Basic
      • JBScreen LCP
      • JBScreen Membrane
      • JBScreen Kinase
      • JBScreen Nuc-Pro
      • JBScreen PEG/Salt
      • JBScreen Pentaerythritol
      • JBScreen PACT++
      • JBScreen JCSG++
      • Pi-Screens
      • JBScreen Wizard
      • Individual JBScreen Conditions
    • Thermofluor Screens
    • Detergent Screens
    • Additive Screens
    • Buffer Screens
    • Solubility & Stability Screens
    • Plates & Accessories
    • Oils & Dyes
  • Screening Membrane Proteins
  • Optimization
  • Data Collection
  • Phasing
  • Cryo-EM

You are here: Crystallography & Cryo-EM | Screening | Crystal Screens

Crystal Screens

JBScreen Family

  • XP Screen
    An optimized JBScreen Basic complemented with the universal additive TEW as “glue” for protein molecules
  • JBScreen Classic
    The JBScreen Classic Kits 1-10 cover 240 (10 kits x 24 conditions each) of the most prominent conditions for protein crystallization. Their compositions result from mining of literature data of several thousands of crystallized proteins. JBScreen represents the selected statistically most successful buffers that yielded protein crystals suitable for X-ray diffraction.
  • JBScreen Basic
    Based on the classic sparse matrix crystallization screen published first by Jancarik and Kim in 1991, it contains 96 unique reagent mixtures for screening a wide range of pH and various salts and precipitants.
  • JBScreen LCP
    An LCP screen based on successfully crystallized integral membrane proteins in the Lipidic Cubic Phase.
  • JBScreen Membrane
    The optimized screen for hydrophobic and membrane proteins
  • JBScreen Kinase
    A highly effective crystallization screen based on data analyses of published kinase structures
  • JBScreen Nuc-Pro
    A highly effective sparse matrix screen based upon extensive screening of the PDB, with focus on entries by structural genomic initiatives, the BMCD and other protocols.
  • JBScreen PEG/Salt
    Efficient screening of PEG 3350 and PEG 5000 MME versus 48 different salts
  • JBScreen Pentaerythritol
    A systematic crystallization screen based on pentaerythritol polymers as precipitants developed by Ulrike Demmer from the Max-Planck-Institute for Biophysics in Frankfurt.
  • JBScreen PACT ++
    Systematic screen for pH, anion, cation testing in the presence of polyehtylene glycol
  • JBScreen JCSG ++
    Optimized sparse matrix screen developed by the Joint Center for Structural Genomics (JCSG)
  • Pi-Screens
    Developed at the MRC Cambridge – Crystallization Screens for soluble and integral membrane proteins based on Pi sampling strategy
  • JBScreen Wizard
    A highly effective random sparse matrix screen for crystallizing proteins, peptides, nucleic acids and macromolecular complexes

Individual Screen Conditions

  • Individual JBScreen conditions are available for all screens of the JBScreen Family

jena–Thermofluor Screens

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Crystallography & Cryo-EM
  • Get started
  • Screening
    • Fragment Screen
    • XP Screens
    • Crystal Screens
    • Thermofluor Screens
    • Detergent Screens
    • Additive Screens
    • Buffer Screens
    • Solubility & Stability Screens
    • Plates & Accessories
    • Oils & Dyes
  • Screening Membrane Proteins
  • Optimization
  • Data Collection
  • Phasing
  • Cryo-EM

You are here: Crystallography & Cryo-EM | Screening | Thermofluor Screens
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Thermofluor Screens

Thermofluor Screens

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.

Example: Stabilizing effects on α-Chymotrypsinogen A are directly correlated with crystallizability

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:

  • without any specific ion
  • with 20 mM CaCl2
  • with 10 mM FeCl3
Thermofluor Screens

Crystal growth was promoted by the stabilizing specific ions CaCl2 & FeCl3 from JBScreen Thermofluor SPECIFIC.

Protein Crystallization: Simply grab the needle from the haystack

Talk held at HEC19 in Warberg, September 29th, 2016

 
Thermofluor ScreensSlides of the talk
 
Thermofluor ScreensFlyer JBScreen Thermofluor
Thermofluor ScreensAnalytik Jena Application Note: Using JBScreen Thermofluor Fundament and Specific on Analytik Jena’s qTOWER3.

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
 

References

  • Ericsson et al. (2006) Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal. Biochem. 357(2):289.
  • Reinhard et al. (2013) Optimization of protein buffer cocktails using Thermofluor. Acta Cryst. F 69:209.
  • Niesen et al. (2007) The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability. Nat. Protoc. 2(9):2212.
  • http://www.rcsb.org/pdb/home/home.do

  • without any specific ion
  • with 20 mM CaCl2
  • with 10 mM FeCl3
Thermofluor ScreensSlides of the talk
Thermofluor ScreensFlyer JBScreen Thermofluor
Thermofluor ScreensAnalytik Jena Application Note: Using JBScreen Thermofluor Fundament and Specific on Analytik Jena’s qTOWER3.

jena–Detergent Screens

上海金畔生物代理jena品牌蛋白结晶试剂耗材工具等,我们将竭诚为您服务,欢迎访问jena官网或者咨询我们获取更多相关jena品牌产品信息。

Crystallography & Cryo-EM
  • Get started
  • Screening
    • Fragment Screen
    • XP Screens
    • Crystal Screens
    • Thermofluor Screens
    • Detergent Screens
    • Additive Screens
    • Buffer Screens
    • Solubility & Stability Screens
    • Plates & Accessories
    • Oils & Dyes
  • Screening Membrane Proteins
  • Optimization
  • Data Collection
  • Phasing
  • Cryo-EM

You are here: Crystallography & Cryo-EM | Screening | Detergent Screens
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Detergent Screens

Detergent Screens

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:

  • Ionic detergents
  • Non-ionic detergents
  • Zwitterionic detergents
  • Non-detergent Sulfobetaines
  • Synthetic Lipids

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.

Detergent Screens

JBScreen Detergents & Prometheus: A winning team

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.

 
Detergent ScreensNanoTemper Application Note: Thermal Unfolding of Membrane Proteins

Products & Ordering

JBScreen Detergents 1 CS-521
 

JBScreen Detergents 2 CS-522
 

JBScreen Detergents 3 CS-523
 

JBScreen Detergents 4 CS-524
 

JBScreen Detergents HTS CS-525
 

JBScreen Membrane 1 – 4 & JBScreen Detergents HTS CS-308
 

References

[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

Selected Literature Citation of JBScreen Detergents

  • Hofmann et al. (2020) High-Level Expression, Purification and Initial Characterization of Recombinant Arabidopsis Histidine Kinase AHK1. Plants 9(3):304.
  • Delle Bovi et al. (2017) Expression and purification of functional insulin and insulin-like growth factor 1 holoreceptors from mammalian cells. Anal. Biochem. DOI 10.1016/j.ab.2017.08.011.

Detergent ScreensNanoTemper Application Note: Thermal Unfolding of Membrane Proteins
  • Hofmann et al. (2020) High-Level Expression, Purification and Initial Characterization of Recombinant Arabidopsis Histidine Kinase AHK1. Plants 9(3):304.
  • Delle Bovi et al. (2017) Expression and purification of functional insulin and insulin-like growth factor 1 holoreceptors from mammalian cells. Anal. Biochem. DOI 10.1016/j.ab.2017.08.011.

jena–Additive Screens

上海金畔生物代理jena品牌蛋白结晶试剂耗材工具等,我们将竭诚为您服务,欢迎访问jena官网或者咨询我们获取更多相关jena品牌产品信息。

Crystallography & Cryo-EM
  • Get started
  • Screening
    • Fragment Screen
    • XP Screens
    • Crystal Screens
    • Thermofluor Screens
    • Detergent Screens
    • Additive Screens
    • Buffer Screens
    • Solubility & Stability Screens
    • Plates & Accessories
    • Oils & Dyes
  • Screening Membrane Proteins
  • Optimization
  • Data Collection
  • Phasing
  • Cryo-EM

You are here: Crystallography & Cryo-EM | Screening | Additive Screens
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Additive Screens

Additive Screens

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.

 
Additive ScreensJBScreen Plus Manual

Products & Ordering

JBScreen Plus Kosmotropic CS-501
 

JBScreen Plus Chaotropic CS-502
 

JBScreen Plus Salts CS-503
 

JBScreen Plus Additives CS-504
 

JBScreen Plus Volatiles CS-505
 

JBScreen Plus Complete CS-506
all 5 JBScreen Plus kits for a special price

JBScreen Plus HTS CS-507L
 

Recommended reading

  • Herberhold et al. (2004) Effects of Chaotropic and Kosmotropic Cosolvents on the Pressure-Induced Unfolding and Denaturation of Proteins: An FT-IR Study on Staphylococcal Nuclease. Biochemistry 43:3336.
  • Batchelor et al. (2004) Impact of protein denaturants and stabilizers on water structure. J. Am. Chem. Soc. 126:1958.
  • Boström et al. (2003) Specific ion effects: Why the properties of lysozyme in salt solutions follow a Hofmeister series. Biophys. J. 85:686.
  • Uedaira et al. (2001) Role of hydration of polyhydroxy compounds in biological systems. Cell. Mol. Biol. 47:823.
  • http://www.lsbu.ac.uk/water/kosmos.html
  • Cacace et al. (1997): The Hofmeister series: salt and solvent effects on interfacial phenomena. Quarterly Reviews of Biophysics 30:241.
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