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Crystallization and preliminary X-ray diffraction analysis of mouse prostaglandin F2α synthase, AKR1B3
Yasuhide Takashima1, Seika Hatanaka, Eiichi Mizohata
1Department of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita, Osaka, Japan.
Abstract:
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 P4(1)2(1)2 or P4(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.
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