Abstract
Alanine racemase (DadXOF4), a dimeric endogenous PLP-dependent alkaline enzyme from alkaliphilic Bacillus pseudofirmus OF4, was expressed in Escherichia coli 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 291 K using a solution containing 1.4 M sodium/potassium phosphate pH 8.2. The protein crystallized in space group P212121, with two protein molecules in the asymmetric unit. © International Union of Crystallography 2009.
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Ju, J., Qi, J., Xu, S., Ohnishi, K., Benedik, M. J., Xue, Y., & Ma, Y. (2009). Crystallization and preliminary X-ray study of alkaline alanine racemase from Bacillus pseudofirmus OF4. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 65(2), 166–168. https://doi.org/10.1107/S174430910900013X
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