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Crystal Screens - JBScreen Classic

JBScreen bulk & HTS

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.


Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes.

Selected Recent Literature Citations of JBScreen Classic

  • Songsiriritthigul et al. (2017) Crystal structure of the N-terminal anticodon-binding domain of the nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori. Acta Cryst F 73:62.
  • McPhail et al. (2017) The Molecular Basis of Aichi Virus 3A Protein Activation of Phosphatidylinositol 4 Kinase IIIβ, PI4KB, through ACBD3. Structure 25:121.
  • García Caballero et al. (2016) Galectin-related protein: An integral member of the network of chicken galectins 1. From strong sequence conservation of the gene confined to vertebrates to biochemical characteristics of the chicken protein and its crystal structure. Biochim Biophys Acta. 1860:2285.
  • Demmer et al. (2015) Insights into Flavin-based Electron Bifurcation via the NADH-dependent Reduced Ferredoxin:NADP Oxidoreductase Structure. JBC 290:21985.
  • Bosshart et al. (2015) Directed Divergent Evolution of a Thermostable d-Tagatose Epimerase towards Improved Activity for Two Hexose Substrates. ChemBioChem 16:592.
  • Sáez-Jiménez et al. (2015) Improving the pH-stability of Versatile Peroxidase by Comparative Structural Analysis with a Naturally-Stable Manganese Peroxidase. PLOS ONE DOI:10.1371/journal.pone.0140984.
  • Liu et al. (2015) Expression, refolding, purification and crystallization of the sensory domain of the TlpC chemoreceptor from Helicobacter pylori for structural studies. Protein Expression and Purification 107:29.
  • Lei et al. (2015) Recombinant expression, purification, crystallization and preliminary X-ray diffraction analysis of Haemophilus influenzae BamD and BamCD complex. Acta Cryst F 71:234.
  • Butryn et al. (2015) Serendipitous crystallization and structure determination of cyanase (CynS) from Serratia proteamaculans. Acta Cryst F 71:471.
  • Chitnumsub et al. (2014) The structure of Plasmodium falciparum serine hydroxymethyltransferase reveals a novel redox switch that regulates its activities. Acta Cryst D 70:1517.
  • Serer et al. (2014) Crystallographic and kinetic study of riboflavin synthase from Brucella abortus, a chemotherapeutic target with an enhanced intrinsic flexibility. Acta Cryst D 70:1419.