Open AccessCrystallization and preliminary X‐ray crystallographic analysis of a carbonyl reductase from Candida parapsilosis
Author(s) -
Zhang Rongzhen,
Xu Yan,
Sun Ying,
Nie Yao,
Mu Xiaoqing,
Li Xuemei,
Zhang Xuejun C.,
Rao Zhihe
Publication year - 2008
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108004132
Subject(s) - crystallography , crystallization , candida parapsilosis , crystal (programming language) , crystal structure , chemistry , polyethylene glycol , materials science , stereochemistry , organic chemistry , antifungal , medicine , dermatology , programming language , computer science
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 × 0.3 × 0.4 mm and diffracted to a resolution of 2.7–3.0 Å. The crystal forms both belong to space group P 2 1 2 1 2 1 and have unit‐cell parameters a = 104.7, b = 142.8, c = 151.8 Å and a = 101.1, b = 146.0, c = 159.8 Å. 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.