大肠杆菌半胱氨酰-tRNA合成酶的结晶及初步衍射分析
Crystallization and preliminary diffraction analysis of Escherichia coli cysteinyl-tRNA synthetase.
作者信息
Newberry K J, Kohn J, Hou Y M, Perona J J
机构信息
Department of Chemistry and Interdepartmental Program in Biochemistry and Molecular Biology, University of California at Santa Barbara, Santa Barbara CA 93106-9510, USA.
出版信息
Acta Crystallogr D Biol Crystallogr. 1999 May;55(Pt 5):1046-7. doi: 10.1107/s0907444999001468.
Crystals of the 52 kDa monomeric Escherichia coli cysteinyl-tRNA synthetase complexed with ATP and cysteine have been grown by hanging-drop vapor diffusion from solutions containing ammonium sulfate as the precipitating agent. The crystals form long hexagonal rods in the space group P321 with unit-cell dimensions a = b = 82.3, c = 168.9 A. There is one enzyme molecule in the asymmetric unit. A complete native data set has been collected from a rotating-anode source to a resolution of 2.7 A at 103 K, with an Rmerge of 6.7%.
52 kDa单体大肠杆菌半胱氨酰 - tRNA合成酶与ATP和半胱氨酸复合的晶体，通过悬滴气相扩散法，从含有硫酸铵作为沉淀剂的溶液中生长而成。晶体在空间群P321中形成长六边形棒，晶胞参数a = b = 82.3，c = 168.9 Å。不对称单元中有一个酶分子。在103 K下，使用旋转阳极源收集了一套完整的天然数据集，分辨率达到2.7 Å，Rmerge为6.7%。
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