Literature DB >> 1409560

Overproduction, crystallization, and preliminary X-ray diffraction studies of the major cold shock protein from Bacillus subtilis, CspB.

H Schindelin1, M Herrler, G Willimsky, M A Marahiel, U Heinemann.   

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.

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Year:  1992        PMID: 1409560     DOI: 10.1002/prot.340140113

Source DB:  PubMed          Journal:  Proteins        ISSN: 0887-3585


  10 in total

1.  Single-stranded DNA binding of the cold-shock protein CspB from Bacillus subtilis: NMR mapping and mutational characterization.

Authors:  Markus Zeeb; Jochen Balbach
Journal:  Protein Sci       Date:  2003-01       Impact factor: 6.725

2.  Effect of pH and phosphate ions on self-association properties of the major cold-shock protein from Bacillus subtilis.

Authors:  G I Makhatadze; M A Marahiel
Journal:  Protein Sci       Date:  1994-11       Impact factor: 6.725

3.  RNA single strands bind to a conserved surface of the major cold shock protein in crystals and solution.

Authors:  Rolf Sachs; Klaas E A Max; Udo Heinemann; Jochen Balbach
Journal:  RNA       Date:  2011-11-29       Impact factor: 4.942

4.  Characterization of cspB, a Bacillus subtilis inducible cold shock gene affecting cell viability at low temperatures.

Authors:  G Willimsky; H Bang; G Fischer; M A Marahiel
Journal:  J Bacteriol       Date:  1992-10       Impact factor: 3.490

5.  Induction of cold shock proteins in Bacillus subtilis.

Authors:  E A Lottering; U N Streips
Journal:  Curr Microbiol       Date:  1995-04       Impact factor: 2.188

Review 6.  Cold-Shock Domains-Abundance, Structure, Properties, and Nucleic-Acid Binding.

Authors:  Udo Heinemann; Yvette Roske
Journal:  Cancers (Basel)       Date:  2021-01-07       Impact factor: 6.639

7.  Sequence specificity of single-stranded DNA-binding proteins: a novel DNA microarray approach.

Authors:  Hugh P Morgan; Peter Estibeiro; Martin A Wear; Klaas E A Max; Udo Heinemann; Liza Cubeddu; Maurice P Gallagher; Peter J Sadler; Malcolm D Walkinshaw
Journal:  Nucleic Acids Res       Date:  2007-05-08       Impact factor: 16.971

Review 8.  Mechanisms of Lin28-mediated miRNA and mRNA regulation--a structural and functional perspective.

Authors:  Florian Mayr; Udo Heinemann
Journal:  Int J Mol Sci       Date:  2013-08-09       Impact factor: 5.923

9.  What does fluorine do to a protein? Thermodynamic, and highly-resolved structural insights into fluorine-labelled variants of the cold shock protein.

Authors:  Hannah Welte; Tiankun Zhou; Xenia Mihajlenko; Olga Mayans; Michael Kovermann
Journal:  Sci Rep       Date:  2020-02-14       Impact factor: 4.379

10.  Insights into Protein Stability in Cell Lysate by 19 F NMR Spectroscopy.

Authors:  Hannah Welte; Michael Kovermann
Journal:  Chembiochem       Date:  2020-09-16       Impact factor: 3.164

  10 in total

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