JBScreen Basic

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 that is deliberately focused on conditions that have proven successful in the crystallization of biological macromolecules.

In 1991, Jancarik and Kim published 50 conditions 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 for the 24-well plate format, and as with all other JBScreen crystallization kits, we have eliminated the use of cacodylate buffers and replaced them with MES. JBScreen Basic contains 96 unique reagent mixtures for screening a wide pH range and various salts and precipitating agents.

Format

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

Products & Ordering

JBScreen Basic 1 CS-121

JBScreen Basic 2 CS-122

JBScreen Basic 3 CS-123

JBScreen Basic 4 CS-124

JBScreen Basic Set 1 - 4 CS-125

JBScreen Basic 1 - 4 HTS CS-203L

BIOZ Product Citations

Please click the arrow on the right to expand the citation list. Click publication title for the full text.

Selected Literature

Ferrero et al. (2021) Snapshots of a Non‐Canonical RdRP in Action. Viruses 13:1260.
Tassone et al. (2021) Validation of Recombinant Chicken Liver Bile Acid Binding Protein as a Tool for Cholic Acid Hosting. Biomolecules 11:645.
Pappas et al. (2020) Emergence of low-symmetry foldamers from single monomers. Nature Chemistry 12:1180.
Corvaglia et al. (2019) Carboxylate-functionalized foldamer inhibitors of HIV-1 integrase and Topoisomerase 1: artificialanalogues of DNA mimic proteins. Nucleic Acids Research DOI:10.1093/nar/gkz352.
Deka et al. (2017) Comparative structural and enzymatic studies on Salmonella typhimurium diaminopropionate ammonia lyase reveal its unique features. J. Struct. Biol. DOI:10.1016/j.jsb.2017.12.012.
Moonens et al. (2015) Structural insight in the inhibition of adherence of F4 fimbriae producing enterotoxigenic Escherichia coli by llama single domain antibodies. Veterinary Research 46:14.
Zano et al. (2014) Structure of an unusual S-adenosylmethionine synthetase from Campylobacter jejuni. Acta Cryst. D 70:442.
Goyal et al. (2013) Crystallization and preliminary X-ray crystallographic analysis of the curli transporter CsgG. Acta Cryst. F 69:1349.

References

[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.