Open AccessCrystallization and preliminary X‐ray study of a thermostable alanine racemase from Thermoanaerobacter tengcongensis MB4
Author(s) -
Dong Hui,
Xu Shujing,
Lu Xiaoyun,
He Guangzheng,
Zhao Ranran,
Chen Shuai,
Fu Sheng,
Ju Jiansong
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113011743
Subject(s) - crystallization , thermophile , alanine , chemistry , biochemistry , crystallography , enzyme , amino acid , organic chemistry
Alanine racemase (Alr MB4 ), a dimeric PLP‐dependent thermostable enzyme from the anaerobic eubacterium Thermoanaerobacter tengcongensis MB4, was expressed 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 289 K using a solution consisting of 0.1 M bis‐tris pH 7.0, 22%( w / v ) polyethylene glycol 4000. X‐ray diffraction data were collected to 2.6 Å resolution. The crystal belonged to the orthorhombic space group P 2 1 2 1 2 1 , with two protein molecules in an asymmetric unit.