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|Title:||Purification, crystallization and preliminary crystallographic analysis of CYP195A2, a P450 enzyme from Rhodopseudomonas palustris|
|Citation:||Protein and Peptide Letters, 2008; 15(4):423-426|
|Publisher:||Bentham Science Publ Ltd|
|Delin Guo, Feng Xu, Stephen G. Bell, Xiaoyun Pang, Mark Bartlam and Luet-Lok Wong|
|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.|
|Keywords:||Cytochrome P450; CYP195A2; Rhodopseudomonas palustris; crystallization|
|Rights:||Copyright status unknown|
|Appears in Collections:||Chemistry and Physics publications|
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