Expression, purification and X-ray analysis of 1,3-propanediol dehydrogenase (Aq_1145) from Aquifex aeolicus VF5.

从嗜热菌 VF5 中表达、纯化和 X 射线分析 1,3-丙二醇脱氢酶 (Aq_1145)

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作者:Jeyakanthan Jeyaraman, Thamotharan Subbiah, Panjikar Santosh, Kitamura Yoshiaki, Nakagawa Noriko, Shinkai Akeo, Kuramitsu Seiki, Yokoyama Shigeyuki
1,3-Propanediol dehydrogenase is an enzyme that catalyzes the oxidation of 1,3-propanediol to 3-hydroxypropanal with the simultaneous reduction of NADP(+) to NADPH. SeMet-labelled 1,3-propanediol dehydrogenase protein from the hyperthermophilic bacterium Aquifex aeolicus VF5 was overexpressed in Escherichia coli and purified to homogeneity. Crystals of this protein were grown from an acidic buffer with ammonium sulfate as the precipitant. Single-wavelength data were collected at the selenium peak to a resolution of 2.4 A. The crystal belonged to space group P3(2), with unit-cell parameters a = b = 142.19, c = 123.34 A. The structure contained two dimers in the asymmetric unit and was solved by the MR-SAD approach.

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