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

A thermostable alanine racemase from T. tengcongensis MB4 was expressed in E. coli and purified. Crystallization and preliminary X-ray crystallographic analysis were performed for the recombinant enzyme. Alanine racemase (Alr_MB4), 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