Protein expression, crystallization and preliminary X-ray crystallographic studies of YJbK from Bacillus subtilis

被引：1

作者：

Dai, XY

Liu, Y

Liang, YH

Zheng, XF

Luo, M

Li, LF

Su, XD ^{[1
]}

机构：

[1] Peking Univ, Coll Life Sci, Natl Lab Prot Engn & Plant Genet Engn, Beijing 100871, Peoples R China

[2] Peking Univ, Coll Life Sci, Dept Biochem & Mol Biol, Beijing 100871, Peoples R China

来源：

PROTEIN AND PEPTIDE LETTERS | 2005年 / 12卷 / 07期

关键词：

B; subtilis; YjbK; protein crystallography;

D O I：

10.2174/0929866054696208

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 angstrom in-house. The crystals belong to P1 space group, with unit cell parameters a=32.38 angstrom, b=34.69 angstrom, c=46.02 angstrom, alpha=96.560 degrees, beta=99.683 degrees, gamma=11.333 degrees. There is one molecule per asymmetric unit.

引用

页码：663 / 664

页数：2

共 5 条

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