来自类芽孢杆菌OF4的碱性丙氨酸消旋酶的结晶及初步X射线研究。
Crystallization and preliminary X-ray study of alkaline alanine racemase from Bacillus pseudofirmus OF4.
作者信息
Ju Jiansong, Qi Jianxun, Xu Shujing, Ohnishi Kouhei, Benedik Michael J, Xue Yanfen, Ma Yanhe
机构信息
State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Feb 1;65(Pt 2):166-8. doi: 10.1107/S174430910900013X. Epub 2009 Jan 31.
Abstract
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.
摘要
丙氨酸消旋酶（DadX(OF4)）是一种来自嗜碱假芽孢杆菌OF4的二聚体内源性磷酸吡哆醛依赖性碱性酶，在大肠杆菌中表达，并通过His(6)标签纯化，得到适合X射线晶体学分析的形式。晶体通过悬滴气相扩散法在291 K下使用含有1.4 M磷酸钠/钾（pH 8.2）的溶液生长。该蛋白质在空间群P2(1)2(1)2(1)中结晶，不对称单位中有两个蛋白质分子。
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