来自嗜酒色杆菌的膜结合[NiFe]氢化酶的纯化、结晶及初步X射线分析。
Purification, crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum.
作者信息
Kellers Petra, Ogata Hideaki, Lubitz Wolfgang
机构信息
Max-Planck-Institut für Bioanorganische Chemie, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Aug 1;64(Pt 8):719-22. doi: 10.1107/S1744309108019945. Epub 2008 Jul 5.
Abstract
The membrane-bound [NiFe] hydrogenase is a unique metalloprotein that is able to catalyze the reversible oxidation of hydrogen to protons and electrons during a complex reaction cycle. The [NiFe] hydrogenase was isolated from the photosynthetic purple sulfur bacterium Allochromatium vinosum and its crystallization and preliminary X-ray analysis are reported. It was crystallized by the hanging-drop vapour-diffusion method using sodium citrate and imidazole as crystallization agents. The crystals belong to space group P2(1)2(1)2, with unit-cell parameters a = 205.00, b = 217.42, c = 120.44 A. X-ray diffraction data have been collected to 2.5 A resolution.
摘要
膜结合[NiFe]氢化酶是一种独特的金属蛋白，在复杂的反应循环中能够催化氢可逆氧化为质子和电子。从光合紫色硫细菌嗜酒色杆菌中分离出了[NiFe]氢化酶，并报道了其结晶及初步X射线分析结果。采用柠檬酸钠和咪唑作为结晶剂，通过悬滴气相扩散法使其结晶。晶体属于空间群P2(1)2(1)2，晶胞参数a = 205.00，b = 217.42，c = 120.44 Å。已收集到分辨率为2.5 Å的X射线衍射数据。
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