Purification, crystallization and preliminary crystallographic analysis of CYP195A2, a P450 enzyme from Rhodopseudomonas palustris
Date
2008
Authors
Guo, D.
Xu, F.
Bell, S.
Pang, X.
Bartlam, M.
Wong, L.
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Protein and Peptide Letters: international journal for rapid publication of short papers in protein and peptide science, 2008; 15(4):423-426
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Delin Guo, Feng Xu, Stephen G. Bell, Xiaoyun Pang, Mark Bartlam and Luet-Lok Wong
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Abstract
Cytochrome P450 monooxygenases are a superfamily of heme-thiolate proteins involved in the metabolism of a wide variety of endogenous and xenobiotic compounds. The P450 enzyme CYP195A2 from Rhodopseudomonas palustris CGA009, a metabolically versatile bacterium, was overproduced in E. coli and purified. Two distinct crystal forms were obtained under separately optimized conditions by the hanging-drop vapor-diffusion method. Native data sets extending to resolutions of 2.3 Å and 2.8 Å have been collected and processed in space groups P222 and C2221 respectively.
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