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Overproduction, crystallization, and preliminary X-ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB.
Proteins. 1992 Sep; 14(1):120-4.P

Abstract

The major cold shock protein from Bacillus subtilis (CspB) was overexpressed using the bacteriophage T7 RNA polymerase/promoter 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 P3(1)21 (P3(2)21) with unit cell dimensions a = b = 59.1 A and c = 46.4 A. The second crystal form is tetragonal, space group P4(1)2(1)2 (P4(3)2(1)2) with unit cell dimensions a = b = 56.9 A and c = 53.0 A. These crystals grow with polyethylene glycol 4000 as precipitant.

Authors+Show Affiliations

Schindelin H
Institut für Kristallographie, Freie Universität Berlin, Federal Republic of Germany.
Herrler M
No affiliation info available
Willimsky G
No affiliation info available
Marahiel MA
No affiliation info available
Heinemann U
No affiliation info available

MeSH

Bacillus subtilisBacterial ProteinsCrystallizationProtein ConformationRecombinant ProteinsX-Ray Diffraction

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

1409560

Citation

Schindelin, H, et al. "Overproduction, Crystallization, and Preliminary X-ray Diffraction Studies of the Major Cold Shock Protein From Bacillus Subtilis, CspB." Proteins, vol. 14, no. 1, 1992, pp. 120-4.
Schindelin H, Herrler M, Willimsky G, et al. Overproduction, crystallization, and preliminary X-ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB. Proteins. 1992;14(1):120-4.
Schindelin, H., Herrler, M., Willimsky, G., Marahiel, M. A., & Heinemann, U. (1992). Overproduction, crystallization, and preliminary X-ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB. Proteins, 14(1), 120-4.
Schindelin H, et al. Overproduction, Crystallization, and Preliminary X-ray Diffraction Studies of the Major Cold Shock Protein From Bacillus Subtilis, CspB. Proteins. 1992;14(1):120-4. PubMed PMID: 1409560.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Overproduction, crystallization, and preliminary X-ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB. AU - Schindelin,H, AU - Herrler,M, AU - Willimsky,G, AU - Marahiel,M A, AU - Heinemann,U, PY - 1992/9/1/pubmed PY - 1992/9/1/medline PY - 1992/9/1/entrez SP - 120 EP - 4 JF - Proteins JO - Proteins VL - 14 IS - 1 N2 - The major cold shock protein from Bacillus subtilis (CspB) was overexpressed using the bacteriophage T7 RNA polymerase/promoter 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 P3(1)21 (P3(2)21) with unit cell dimensions a = b = 59.1 A and c = 46.4 A. The second crystal form is tetragonal, space group P4(1)2(1)2 (P4(3)2(1)2) with unit cell dimensions a = b = 56.9 A and c = 53.0 A. These crystals grow with polyethylene glycol 4000 as precipitant. SN - 0887-3585 UR - https://www.unboundmedicine.com/medline/citation/1409560/Overproduction_crystallization_and_preliminary_X_ray_diffraction_studies_of_the_major_cold_shock_protein_from_Bacillus_subtilis_CspB_ DB - PRIME DP - Unbound Medicine ER -