来自集胞藻属蓝细菌PCC 6803的同二聚体甘氨酸脱羧酶（P蛋白）的结晶及初步X射线衍射分析。
Crystallization and preliminary X-ray diffraction analyses of the homodimeric glycine decarboxylase (P-protein) from the cyanobacterium Synechocystis sp. PCC 6803.
作者信息
Hasse Dirk, Hagemann Martin, Andersson Inger, Bauwe Hermann
机构信息
Department of Plant Physiology, University of Rostock, Germany.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):187-91. doi: 10.1107/S1744309109052828. Epub 2010 Jan 28.
Abstract
Glycine decarboxylase, or P-protein, is a major enzyme that is involved in the C(1) metabolism of all organisms and in the photorespiratory pathway of plants and cyanobacteria. The protein from Synechocystis sp. PCC 6803 is a homodimer with a mass of 215 kDa. Recombinant glycine decarboxylase was expressed in Escherichia coli and purified by metal-affinity, ion-exchange and gel-filtration chromatography. Crystals of P-protein that diffracted to a resolution of 2.1 A were obtained using the hanging-drop vapour-diffusion method at 291 K. X-ray diffraction data were collected from cryocooled crystals using synchrotron radiation. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 96.30, b = 135.81, c = 179.08 A.
摘要
甘氨酸脱羧酶，即P蛋白，是一种主要的酶，参与所有生物体的C(1)代谢以及植物和蓝细菌的光呼吸途径。来自集胞藻属PCC 6803的该蛋白是一种质量为215 kDa的同型二聚体。重组甘氨酸脱羧酶在大肠杆菌中表达，并通过金属亲和、离子交换和凝胶过滤色谱法进行纯化。使用悬滴气相扩散法在291 K下获得了衍射分辨率为2.1 Å的P蛋白晶体。使用同步辐射从低温冷却的晶体收集X射线衍射数据。晶体属于空间群P2(1)2(1)2(1)，晶胞参数a = 96.30，b = 135.81，c = 179.08 Å。
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