Purification, Crystallization and Preliminary Crystallographic Analysis of CYP 195A2, a P450 Enzyme from Rhodopseudomonas palustris

Title: Purification, Crystallization and Preliminary Crystallographic Analysis of CYP 195A2, a P450 Enzyme from Rhodopseudomonas palustris

Volume: 15 Issue: 4

Author(s): Delin Guo, Feng Xu, Stephen G. Bell, Xiaoyun Pang, Mark Bartlam and Luet-Lok Wong

Affiliation:

Keywords: Cytochrome P450, CYP195A2, Rhodopseudomonas palustris, crystallization

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.

Cite this article as:

Guo Delin, Xu Feng, Bell G. Stephen, Pang Xiaoyun, Bartlam Mark and Wong Luet-Lok, Purification, Crystallization and Preliminary Crystallographic Analysis of CYP 195A2, a P450 Enzyme from Rhodopseudomonas palustris, Protein & Peptide Letters 2008; 15 (4) . https://dx.doi.org/10.2174/092986608784246470