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Crystallization and preliminary X-ray crystallographic analysis of a carbonyl reductase from Candida parapsilosis.

Authors
Type
Published Article
Journal
Acta Crystallographica Section F Structural Biology and Crystallization Communications
1744-3091
Publisher
International Union of Crystallography
Publication Date
Volume
64
Issue
Pt 4
Pages
252–254
Identifiers
DOI: 10.1107/S1744309108004132
PMID: 18391419
Source
Medline
License
Unknown

Abstract

A novel short-chain NADPH-dependent (S)-1-phenyl-1,2-ethanediol dehydrogenase (SCR) has been crystallized. Two distinct but related crystal forms of SCR were obtained using the hanging-drop vapour-diffusion method and a reservoir solution consisting of 18%(w/v) polyethylene glycol 2000 monomethyl ether and 8%(v/v) 2-propanol as the precipitant. The crystals were rhomboid in shape with average dimensions of 0.3 x 0.3 x 0.4 mm and diffracted to a resolution of 2.7-3.0 A. The crystal forms both belong to space group P2(1)2(1)2(1) and have unit-cell parameters a = 104.7, b = 142.8, c = 151.8 A and a = 101.1, b = 146.0, c = 159.8 A. The calculated values of V(M), rotation-function and translation-function solutions and consideration of potential crystal packing suggest that there are eight protein subunits per asymmetric unit.

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