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. Please follow this link.

   Description how the JBScreen buffers are prepared

   More background information on JBScreen Classic

• Marcia et al. (2009) The structure of Aquifex aeolicus sulfide:quinone oxidoreductase, a basis to understand sulfide detoxification and respiration. Proc. Natl. Acad. Sci. 106:9625.
• Dunstan et al. (2009) Structure of the Thiostrepton Resistance Methyltransferase S-Adenosyl-L-methionine Complex and Its Interaction with Ribosomal RNA. J. Biol. Chem. 284:17013.
• Sugishima et al. (2009) Crystal Structure of Red Chlorophyll Catabolite Reductase: Enlargement of the Ferredoxin-Dependent Bilin Reductase Family J. Mol. Biol. 389:376.
• Vulliez-LeNormand et al. (2008) Structures of synthetic O-antigen fragments from serotype 2a Shigella flexneri in complex with a protective monoclonal antibody. Proc. Natl. Acad. Sci. 105:9976.
• Okada et al. (2007) Crystal Structure of the γ-Glutamyltranspeptidase Precursor Protein from Escherichia coli. J. Biol Chem. 282:2433.
• Smatanova´ et al. (2006) New techniques for membrane protein crystallization tested on photosystem II core complex of Pisum sativum. Photosynth. Res. 90:255.
• Ferraroni et al. (2005) Crystallization and preliminary structure analysis of the blue laccase from the ligninolytic fungus Panus tigrinus. Acta Cryst. F 61:205.
• Cherezov et al. (2004) A robotic system for crystallizing membrane and soluble proteins in lipidic mesophases. Acta Cryst. D 60:1795.
• Irimia et al. (2004) Methanoarchaeal sulfolactate dehydrogenase: prototype of a new family of NADH-dependent enzymes. EMBO J. 23:1234.
• Vallazza et al. (2004) First look at RNA in L-configuration. Acta Cryst. D 60:1.
• Kundrot (2004) Which strategy for a protein crystallization project? Cell. Mol. Life Sci. 61:525.
• Unciuleac et al. (2004) Crystallization of 4-hydroxybenzoyl-CoA reductase and the structure of its electron donor ferredoxin. Acta Cryst. D 60:388.
• Vorup-Jensen et al. (2003) Structure and allosteric regulation of the aXb2 integrin I domain. Proc. Natl. Acad. Sci. USA 100:1873.

Please contact xtals@jenabioscience.com with questions or inquiries.