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. Each condition of the four kits is supplied in 10 ml quantities. For high-throughput users, we offer all 96 conditions in pre-filled deep well blocks.

Individual Conditions of all screens are available in 10 ml as well as 100 ml volumes. Please follow this link.

   Why cacodylate is bad medicine

   Description how the JBScreen buffers are prepared

[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.

• Kumar et al. (2009) Crystallization and preliminary X-ray diffraction analysis of human seminal plasma protein PSP94. Acta Cryst. F 65:389.
• Squina et al. (2009) Expression, purification, crystallization and preliminary crystallographic analysis of an endo-1,5-α-L-arabinanase from hyperthermophilic Thermotoga petrophila. Acta Cryst. F 65:902.
• Feahnle et al. (2006) Examination of Key Intermediates in the Catalytic Cycle of Aspartate-β-semialdehyde Dehydrogenase from a Gram-positive Infectious Bacteria. J. Biol. Chem. 281:31031.
• Küttener et al. (2006) Crystallization and preliminary X-ray characterization of two thermostable DNA nucleases. Acta Cryst. F 62:1290.

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