Crystallization and preliminary X‐ray study of a thermostable alanine racemase from Thermoanaerobacter tengcongensis MB4. Issue 6 (31st May 2013)

• Record Type: Journal Article
• Authors: Dong, Hui; Xu, Shujing; Lu, Xiaoyun; He, Guangzheng; Zhao, Ranran; Chen, Shuai; Fu, Sheng; Ju, Jiansong
• Is Part Of: Acta crystallographica. Volume 69:Issue 6(2013:Jun.)
• Page Start: 660
• Page End: 662
• Publication Date: 2013-05-31
• Subjects: Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S1744309113011743
• Languages: English
• ISSNs: 1744-3091

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>Alanine racemase (Alr_MB4), a dimeric PLP‐dependent thermostable enzyme from the anaerobic eubacterium <italic>Thermoanaerobacter tengcongensis</italic> 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 <italic>M</italic> bis‐tris pH 7.0, 22%(<italic>w</italic>/<italic>v</italic>) polyethylene glycol 4000. X‐ray diffraction data were collected to 2.6 Å resolution. The crystal belonged to the orthorhombic space group <italic>P</italic>2₁2₁2₁, with two protein molecules in an asymmetric unit.</p> </abstract>