title: Purification, crystallization and preliminary crystallographic analysis of CYP 195A2, a P450 enzyme from Rhodopseudomonas palustris.
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.
authors.affiliation: Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing, 100084, China.
authors.forename: Delin
authors.initials: D
authors.lastname: Guo
authors.forename: Feng
authors.initials: F
authors.lastname: Xu
authors.forename: Stephen G
authors.initials: SG
authors.lastname: Bell
authors.forename: Xiaoyun
authors.initials: X
authors.lastname: Pang
authors.forename: Mark
authors.initials: M
authors.lastname: Bartlam
authors.forename: Luet-Lok
authors.initials: LL
authors.lastname: Wong
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000302:isolation & purification*; D012241:Rhodopseudomonas / Q000201:enzymology*
chemical_list: D003577:Cytochrome P-450 Enzyme System