Related Experiment Video
Updated: Jun 25, 2026

Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Crystallization and preliminary X-ray study of alkaline alanine racemase from Bacillus pseudofirmus OF4
Jiansong Ju1, Jianxun Qi, Shujing Xu
1State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, People's Republic of China.
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.

