Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009

Peng, Y.
Xu, F.
Bell, S.
Wong, L.
Rao, Z.

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Publication date

January 2007

DOI

10.1107/S1744309107017411

Publisher

International Union of Crystallography (IUCr)

ISSN

1744-3091

Journal

Acta Crystallographica Section F Structural Biology and Crystallization Communications

Abstract

Palustrisredoxin reductase from Rhodopseudomonas palustris CGA009, a member of the oxygenase-coupled NADH-dependent ferredoxin reductase (ONFR) family, catalyzes electron transfer from NADH to ferredoxins. It is an essential component of the cytochrome P450 systems in R. palustris CGA009, a model organism with diverse metabolic pathways. Here, the crystallization of palustrisredoxin reductase is reported. The crystals belong to the trigonal space group P3₂21, with unit-cell parameters a = 107.5, b = 107.5, c = 69.9 Å, and diffract to 2.2 Å resolution on a synchrotron source.Ying Peng, Feng Xu, Stephen G. Bell, Luet-Lok Wong and Zihe Ra

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Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009

Abstract

Extracted data

Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009

Abstract

Extracted data

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