Jeyakanthan Jeyaraman, Thamotharan Subbiah, Panjikar Santosh, Kitamura Yoshiaki, Nakagawa Noriko, Shinkai Akeo, Kuramitsu Seiki, Yokoyama Shigeyuki
National Synchrotron Radiation Research Center, 101 Hsin-Ann Road, Hsinchu Science Park, Hsinchu 30076, Taiwan.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):184-6. doi: 10.1107/S1744309109052403. Epub 2010 Jan 28.
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.
1,3-丙二醇脱氢酶是一种催化1,3-丙二醇氧化为3-羟基丙醛，同时将NADP(+)还原为NADPH的酶。来自嗜热细菌嗜泉古菌VF5的硒代甲硫氨酸标记的1,3-丙二醇脱氢酶蛋白在大肠杆菌中过表达并纯化至同质。该蛋白的晶体从含有硫酸铵作为沉淀剂的酸性缓冲液中生长。在硒峰处收集单波长数据，分辨率为2.4 Å。晶体属于空间群P3(2)，晶胞参数a = b = 142.19，c = 123.34 Å。该结构在不对称单元中包含两个二聚体，并通过MR-SAD方法解析。
