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Protein Expression, Crystallization and Preliminary X-Ray Crystallographic Studies of YjbK from Bacillus subtilis

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Abstract:

B. subtilis YjbK is a protein with 190 residues of uncharacterized function, it has been annotated by Pfam database as a member of adenylate cyclase family (EC: 4.6.1.1). In order to identify its exact function via structural studies, yjbK gene was amplified from B. subtilis genomic DNA and cloned into expression vector pET21-DEST. The protein was expressed in a soluble form in E. coli and purified to homogeneity. YjbK was crystallized and diffracted to a resolution of 2.0 Å in-house. The crystals belong to P1 space group, with unit cell parameters a=32.38 Å, b=34.69 Å, c=46.02 Å, α=96.560 , β=99.683° , γ=111.333° . There is one molecule per asymmetric unit.

Keywords: Yjbk; b. subtilis; protein crystallography

Document Type: Review Article

DOI: http://dx.doi.org/10.2174/0929866054696208

Affiliations: National Laboratory of Protein Engineering and Plant Genetic Engineering, China;

Publication date: October 1, 2005

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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