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

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

Volume: 12 Issue: 7

Author(s): Xue-Yu Dai, Yuan Liu, Yu-He Liang, Xiaofeng Zheng, Ming Luo, Lanfen Li and Xiao-Dong Su

Affiliation:

Keywords: b. subtilis, Yjbk, protein crystallography

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.

Cite this article as:

Dai Xue-Yu, Liu Yuan, Liang Yu-He, Zheng Xiaofeng, Luo Ming, Li Lanfen and Su Xiao-Dong, Protein Expression, Crystallization and Preliminary X-Ray Crystallographic Studies of YjbK from Bacillus subtilis, Protein & Peptide Letters 2005; 12 (7) . https://dx.doi.org/10.2174/0929866054696208