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Acta Crystallogr Sect F Struct Biol Cryst Commun. May 1, 2007; 63(Pt 5): 422–425.
Published online Apr 20, 2007. doi:  10.1107/S1744309107017411
PMCID: PMC2335014
Crystallization and preliminary X-ray diffraction studies of a ferredoxin reductase from Rhodopseudomonas palustris CGA009
Ying Peng,a Feng Xu,a* Stephen G. Bell,b Luet-Lok Wong,b* and Zihe Raoac
aLaboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing 100084, People’s Republic of China
bDepartment of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford OX1 3QR, England
cNational Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese Academy of Sciences, Beijing 100101, People’s Republic of China
Correspondence e-mail: xuf/at/xtal.tsinghua.edu.cn, luet.wong/at/chem.ox.ac.uk
Received March 5, 2007; Accepted April 9, 2007.
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.
Articles from Acta Crystallographica Section F: Structural Biology and Crystallization Communications are provided here courtesy of
International Union of Crystallography