Crystallization and preliminary X-ray study of alkaline alanine racemase from Bacillus pseudofirmus OF4

被引：3

作者：

Ju, Jiansong ^{[1
]}

Qi, Jianxun ^{[2
]}

Xu, Shujing ^{[3
]}

Ohnishi, Kouhei ^{[4
]}

Benedik, Michael J. ^{[5
]}

Xue, Yanfen ^{[1
]}

Ma, Yanhe ^{[1
]}

机构：

[1] Chinese Acad Sci, Inst Microbiol, State Key Lab Microbial Resources, Beijing 100101, Peoples R China

[2] Chinese Acad Sci, Inst Phys, Beijing 100049, Peoples R China

[3] Shaanxi Univ Sci & Technol, Life Coll Sci & Engn, Xian 710021, Peoples R China

[4] Kochi Univ, Res Inst Mol Genet, Nanko Ku, Kochi 7838502, Japan

[5] Texas A&M Univ, Dept Biol, College Stn, TX 77843 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2009年 / 65卷

基金：

中国博士后科学基金;

关键词：

PURIFICATION; GERMINATION; CRYSTALS;

D O I：

10.1107/S174430910900013X

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Alanine racemase (DadX(OF4)), a dimeric endogenous PLP-dependent alkaline enzyme from alkaliphilic Bacillus pseudofirmus OF4, was expressed in Escherichia coli and purified with a His(6) tag in a form suitable for X-ray crystallographic analysis. Crystals were grown by the hanging-drop vapour-diffusion method at 291 K using a solution containing 1.4 M sodium/potassium phosphate pH 8.2. The protein crystallized in space group P2(1)2(1)2(1), with two protein molecules in the asymmetric unit.

引用

页码：166 / 168

页数：3

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