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Journal article

Cloning, purification, crystallization and preliminary X-ray analysis of a chimeric NADPH-cytochrome P450 reductase.

Abstract:

NADPH-cytochrome P450 reductase (CPR) is the favoured redox partner of microsomal cytochromes P450. This protein is composed of two flavin-containing domains (FMN and FAD) connected by a structured linker. An active CPR chimera consisting of the yeast FMN and human FAD domains has been produced, purified and crystallized. The crystals belonged to the monoclinic space group C2 and contained one molecule per asymmetric unit. Molecular replacement was performed using the published rat and yeast ...

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Publication status:
Published

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Publisher copy:
10.1107/s1744309109000700

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Institution:
University of Oxford
Department:
Oxford, MPLS, Physics
Role:
Author
Journal:
Acta crystallographica. Section F, Structural biology and crystallization communications
Volume:
65
Issue:
Pt 3
Pages:
210-212
Publication date:
2009-03-05
DOI:
EISSN:
1744-3091
ISSN:
1744-3091
URN:
uuid:306dcd08-94e8-4675-8119-e6bf8004737f
Source identifiers:
154792
Local pid:
pubs:154792

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