Crystallization and preliminary X-ray analysis of an alanine dehydrogenase from Bacillus megaterium WSH-002

被引：3
|
作者：
Lu, Xiaoyun [1 ,2 ]
Yi, Qiufen [1 ,2 ]
Zhang, Guofang [1 ,2 ]
Zhu, Xianming [2 ]
Zhou, Honggang [3 ]
Dong, Hui [2 ]
机构：
[1] Tianjin Univ Sci & Technol, Tianjin 300222, Peoples R China
[2] Tianjin Int Joint Acad Biotechnol & Med, Tianjin 300457, Peoples R China
[3] Nankai Univ, Coll Pharm, Tianjin 300071, Peoples R China
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷
基金：
中国国家自然科学基金;
关键词：
MYCOBACTERIUM-TUBERCULOSIS; SUBTILIS; CRYSTALS; MODEL;
D O I：
10.1107/S1744309113019672
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Alanine dehydrogenase (L-AlaDH) from Bacillus megaterium WSH-002 catalyses the NAD(+)-dependent interconversion of L-alanine and pyruvate. The enzyme was expressed in Escherichia coli BL21 (DE3) cells and purified with a His(6) tag by Ni2+-chelating affinity chromatography for X-ray crystallographic analysis. Crystals were grown in a solution consisting of 0.1 M HEPES pH 8.0, 12%(w/v) polyethylene glycol 8000, 8%(v/v) ethylene glycol at a concentration of 15 mg ml(-1) purified protein. The crystal diffracted to 2.35 angstrom resolution and belonged to the trigonal space group R32, with unit-cell parameters a = b = 125.918, c = 144.698 angstrom.
引用
收藏
页码：934 / 936
页数：3
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