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Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris.

ABSTRACT: 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 A 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 A, alpha = beta = gamma = 90 degrees. There is one protein molecule per asymmetric unit.

SUBMITTER: Pang X

PROVIDER: S-EPMC2330210 | biostudies-literature | 2007 Apr

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary crystallographic analysis of cytochrome P450 203A1 from Rhodopseudomonas palustris.

Pang Xiaoyun X Xu Feng F Bell Stephen G SG Guo Delin D Wong Luet Lok LL Rao Zihe Z

Acta crystallographica. Section F, Structural biology and crystallization communications 20070330 Pt 4

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 A resolution f ...[more]

PMID: 17401212

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