Overproduction, crystallization, and preliminary X‐ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB
- 1 September 1992
- journal article
- research article
- Published by Wiley in Proteins-Structure Function and Bioinformatics
- Vol. 14 (1), 120-124
- https://doi.org/10.1002/prot.340140113
Abstract
The major co ld shock protein form Bacillus subtilis (CspB) was voerexressed using the bacteriophage T7 RNA polymerase/promotor system and purified to apparent homogeneity from recombinant Escherichia coli cells. CspB was crystallized in two different forms using vapor diffusion methods. The first crystal form obtained with ammonium sulfate as precipitant belongs to the trigonal crystal system, space group P3121 (P3221) with unit cell dimensions a = b = 59.1 Å and c = 46.4 Å. The second crystal form is tetragonal, space group P41212 (P43212) with unit cell dimensionsa = b = 56.9 Å and c = 53.0 Å. These crystals grow with polyethylene glycol 4000 as precipitant.Keywords
This publication has 13 references indexed in Scilit:
- Identification of a cold shock transcriptional enhancer of the Escherichia coli gene encoding nucleoid protein H-NS.Proceedings of the National Academy of Sciences, 1991
- Sparse matrix sampling: a screening method for crystallization of proteinsJournal of Applied Crystallography, 1991
- Molecular characterization of specific heat shock proteins inBacillus subtilisCurrent Microbiology, 1991
- Cold shock and DNA bindingNature, 1990
- Major cold shock protein of Escherichia coli.Proceedings of the National Academy of Sciences, 1990
- THE HEAT-SHOCK PROTEINSAnnual Review of Genetics, 1988
- Evaluation of single-crystal X-ray diffraction data from a position-sensitive detectorJournal of Applied Crystallography, 1988
- Crystal structure of an antifreeze polypeptide and its mechanistic implicationsNature, 1988
- Crystal orientation and X-ray pattern prediction routines for area-detector diffractometer systems in macromolecular crystallographyJournal of Applied Crystallography, 1987
- A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes.Proceedings of the National Academy of Sciences, 1985