来自大肠杆菌的精氨酰 - tRNA合成酶的结晶及初步X射线衍射分析。
Crystallization and preliminary X-ray diffraction analysis of arginyl-tRNA synthetase from Escherichia coli.
作者信息
Zhou M, Wang E D, Campbell R L, Wang Y L, Lin S X
机构信息
Laboratory of Molecular Endocrinology, CHUL Research Center and Laval University, Québec, Canada.
出版信息
Protein Sci. 1997 Dec;6(12):2636-8. doi: 10.1002/pro.5560061217.
Abstract
Arginyl-tRNA Synthetase, a class I aminoacyl tRNA synthetase playing a crucial role in protein biosynthesis, has been crystallized for the first time. Polyethylene glycol (PEG) was used as a precipitant, and the crystallization proceeded at pH 6.5. These single crystals diffracted to 2.8 A with a rotating anode X-ray source and R-axis IIc image plate detector. They have an orthorhombic space group P2(1)2(1)2 with unit cell parameters of a = 251.51 A, b = 53.12 A, and c = 52.35 A. A complete native data set has been collected at 3.1 A resolution for these crystals.
摘要
精氨酰 - tRNA合成酶是一种在蛋白质生物合成中起关键作用的I类氨酰tRNA合成酶，首次实现了结晶。聚乙二醇（PEG）用作沉淀剂，在pH 6.5条件下进行结晶。这些单晶在旋转阳极X射线源和R轴IIc成像板探测器下衍射至2.8埃。它们属于正交空间群P2(1)2(1)2，晶胞参数为a = 251.51埃，b = 53.12埃，c = 52.35埃。已针对这些晶体在3.1埃分辨率下收集了完整的天然数据集。
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