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Crystallization and preliminary X-ray study of alkaline alanine racemase from Bacillus pseudofirmus OF4.

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.

SUBMITTER: Ju J 

PROVIDER: S-EPMC2635857 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray study of alkaline alanine racemase from Bacillus pseudofirmus OF4.

Ju Jiansong J   Qi Jianxun J   Xu Shujing S   Ohnishi Kouhei K   Benedik Michael J MJ   Xue Yanfen Y   Ma Yanhe Y  

Acta crystallographica. Section F, Structural biology and crystallization communications 20090131 Pt 2

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. ...[more]

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