Open AccessCrystallization and preliminary X‐ray crystallographic studies of pig heart carbonyl reductase
Author(s) -
Aoki Kenichi,
Tanaka Nobutada,
Araki Naoko,
Ishikura Shuhei,
Imamura Yorishige,
Hara Akira,
Nakamura Kazuo T.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106037535
Subject(s) - tetragonal crystal system , crystallography , crystallization , resolution (logic) , crystal (programming language) , reductase , chemistry , crystal structure , diffraction , x ray crystallography , x ray , stereochemistry , materials science , enzyme , optics , physics , biochemistry , organic chemistry , artificial intelligence , computer science , programming language
Pig heart carbonyl reductase (PHCR), which belongs to the short‐chain dehydrogenase/reductase (SDR) family, has been crystallized by the hanging‐drop vapour‐diffusion method. Two crystal forms (I and II) have been obtained in the presence of NADPH. Form I crystals belong to the tetragonal space group P 4 2 , with unit‐cell parameters a = b = 109.61, c = 94.31 Å, and diffract to 1.5 Å resolution. Form II crystals belong to the tetragonal space group P 4 1 2 1 2, with unit‐cell parameters a = b = 120.10, c = 147.00 Å, and diffract to 2.2 Å resolution. Both crystal forms are suitable for X‐ray structure analysis at high resolution.