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Journal article

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 resolutio...

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Publication status:
Published

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Publisher copy:
10.1107/s1744309107012705

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
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Journal:
Acta crystallographica. Section F, Structural biology and crystallization communications
Volume:
63
Issue:
Pt 4
Pages:
342-345
Publication date:
2007-04-05
DOI:
EISSN:
1744-3091
ISSN:
1744-3091
URN:
uuid:34643c68-5c57-4ed5-b4d4-95ce6e130a76
Source identifiers:
40348
Local pid:
pubs:40348

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