Crystallization and preliminary X‐ray analysis of an alanine dehydrogenase from  Bacillus megaterium  WSH‐002 | Zendy

Lu Xiaoyun | Zendy; Yi Qiufen | Zendy; Zhang Guofang | Zendy; Zhu Xianming | Zendy; Zhou Honggang | Zendy; Dong Hui | Zendy

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Crystallization and preliminary X‐ray analysis of an alanine dehydrogenase from Bacillus megaterium WSH‐002

Author(s) -

Lu Xiaoyun,

Yi Qiufen,

Zhang Guofang,

Zhu Xianming,

Zhou Honggang,

Dong Hui

Publication year - 2013

Publication title -

acta crystallographica section f

Language(s) - English

Resource type - Journals

ISSN - 1744-3091

DOI - 10.1107/s1744309113019672

Subject(s) - bacillus megaterium , polyethylene glycol , crystallization , ethylene glycol , escherichia coli , dehydrogenase , alanine , nad+ kinase , chemistry , enzyme , nuclear chemistry , biochemistry , biology , amino acid , bacteria , organic chemistry , gene , genetics

Alanine dehydrogenase (L‐AlaDH) from Bacillus megaterium WSH‐002 catalyses the NAD + ‐dependent interconversion of L‐alanine and pyruvate. The enzyme was expressed in Escherichia coli BL21 (DE3) cells and purified with a His 6 tag by Ni 2+ ‐chelating affinity chromatography for X‐ray crystallographic analysis. Crystals were grown in a solution consisting of 0.1 M HEPES pH 8.0, 12%( w / v ) polyethylene glycol 8000, 8%( v / v ) ethylene glycol at a concentration of 15 mg ml −1 purified protein. The crystal diffracted to 2.35 Å resolution and belonged to the trigonal space group R 32, with unit‐cell parameters a = b = 125.918, c = 144.698 Å.

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