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	Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris
	Pang, Xiaoyun ; Xu, Feng ; Bell, Stephen G. ; Guo, Delin ; Wong, Luet-Lok ; Rao, Zihe
	2010-05-11 ; 2010-05-11
关键词	CRYSTAL-STRUCTURE GENES BIODEGRADATION ENZYMES Biochemical Research Methods Biochemistry & Molecular Biology Biophysics Crystallography
中文摘要	Cytochrome P450 enzymes constitute a large family of haemoproteins that catalyze the monooxygenation of a great variety of endogenous and exogenous organic compounds. Cytochrome P450 203A1 (CYP203A1, RPA1009) from the metabolically versatile organism Rhodopseudomonas palustris binds a broad range of substrates, in particular substituted aromatic compounds. Crystals of CYP203A1 suitable for X-ray crystallography have been obtained and diffraction data were collected in-house to 2.0 angstrom resolution from a single crystal. The crystals belong to space group P222, with unit-cell parameters a = 40.1, b = 95.1, c = 99.0 angstrom, alpha = beta = gamma = 90 degrees. There is one protein molecule per asymmetric unit.
语种	英语 ; 英语
出版者	BLACKWELL PUBLISHING ; OXFORD ; 9600 GARSINGTON RD, OXFORD OX4 2DQ, OXON, ENGLAND
内容类型	期刊论文
源URL	[http://hdl.handle.net/123456789/27549]
专题	清华大学
推荐引用方式 GB/T 7714	Pang, Xiaoyun,Xu, Feng,Bell, Stephen G.,et al. Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris[J],2010, 2010.
APA	Pang, Xiaoyun,Xu, Feng,Bell, Stephen G.,Guo, Delin,Wong, Luet-Lok,&Rao, Zihe.(2010).Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris..
MLA	Pang, Xiaoyun,et al."Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris".(2010).

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