Purification, crystallization and preliminary crystallographic analysis of CYP 195A2, a P450 enzyme from Rhodopseudomonas palustris |
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Authors: | Guo Delin Xu Feng Bell Stephen G Pang Xiaoyun Bartlam Mark Wong Luet-Lok |
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Institution: | Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing, 100084, China. |
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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 A and 2.8 A have been collected and processed in space groups P222 and C2221 respectively. |
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