Crystallization and preliminary X-ray study of a thermostable alanine racemase from Thermoanaerobacter tengcongensis MB4

Abstract

Alanine racemase (AlrMB4), a dimeric PLP-dependent thermostable enzyme from the anaerobic eubacterium Thermoanaerobacter tengcongensis MB4, was expressed and purified with a His6 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 P212121, with two protein molecules in an asymmetric unit. © 2013 International Union of Crystallography. All rights reserved.