Open AccessCrystallization and preliminary X‐ray diffraction analysis of mouse prostaglandin F 2α synthase, AKR1B3
Author(s) -
Takashima Yasuhide,
Hatanaka Seika,
Mizohata Eiichi,
Nagata Nanae,
Fukunishi Yoshifumi,
Matsumura Hiroyoshi,
Urade Yoshihiro,
Inoue Tsuyoshi
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111036165
Subject(s) - crystallization , atp synthase , crystallography , prostaglandin , x ray crystallography , x ray , materials science , chemistry , diffraction , biochemistry , enzyme , physics , optics , organic chemistry
Aldo‐keto reductase 1B3 (AKR1B3) catalyzes the NADPH‐dependent reduction of prostaglandin H 2 (PGH 2 ), which is a common intermediate of various prostanoids, to form PGF 2α . AKR1B3 also reduces PGH 2 to PGD 2 in the absence of NADPH. AKR1B3 produced in Escherichia coli was crystallized in complex with NADPH by the sitting‐drop vapour‐diffusion method. The crystal was tetragonal, belonging to space group P 4 1 2 1 2 or P 4 3 2 1 2, with unit‐cell parameters a = b = 107.62, c = 120.76 Å. X‐ray diffraction data were collected to 2.4 Å resolution at 100 K using a synchrotron‐radiation source.