嗜热栖热菌高电位铁硫蛋白的结晶及初步晶体学分析
Crystallization and preliminary crystallographic analysis of the high-potential iron-sulfur protein from Thermochromatium tepidum.
作者信息
Nogi T, Kobayashi M, Nozawa T, Miki K
机构信息
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606--8502, Japan.
出版信息
Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):656-8. doi: 10.1107/s0907444900003127.
The high-potential iron-sulfur protein (HiPIP) is an electron carrier between the photosynthetic reaction centre and the cytochrome bc(1) complex in the electron-transfer chain of photosynthesis. The purified HiPIP from Thermochromatium tepidum (formerly Chromatium tepidum) was crystallized in a solution of 1.4 M ammonium sulfate and 0.1 M sodium citrate pH 3.5. The crystals diffract X-rays beyond 1.4 A resolution and belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 47.12 (6), b = 59.59 (10), c = 23.62 (3) A. The structure was preliminarily solved by the molecular-replacement method. The crystal structure of HiPIP from T. tepidum showed that the proteins exist as monomers, although HiPIPs from several other species can form dimers.
高电位铁硫蛋白（HiPIP）是光合作用电子传递链中光合反应中心与细胞色素bc(1)复合物之间的电子载体。从嗜温嗜热色菌（原嗜温着色菌）纯化得到的HiPIP在1.4 M硫酸铵和0.1 M柠檬酸钠pH 3.5的溶液中结晶。这些晶体对X射线的衍射分辨率超过1.4 Å，属于正交空间群P2(1)2(1)2(1)，晶胞参数a = 47.12 (6)，b = 59.59 (10)，c = 23.62 (3) Å。该结构通过分子置换法初步解析。嗜温嗜热色菌HiPIP的晶体结构表明，该蛋白以单体形式存在，尽管来自其他几个物种的HiPIP可以形成二聚体。
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