嗜热栖热菌赖氨酰 - tRNA合成酶与其同源tRNAlys以及大肠杆菌tRNAlys的共结晶。
Cocrystallization of lysyl-tRNA synthetase from Thermus thermophilus with its cognate tRNAlys and with Escherichia coli tRNAlys.
作者信息
Yaremchuk A D, Krikliviy I A, Cusack S, Tukalo M A
机构信息
European Molecular Biology Laboratory, Grenoble Outstation, France.
出版信息
Proteins. 1995 Mar;21(3):261-4. doi: 10.1002/prot.340210309.
Lysyl-tRNA synthetase from Thermus thermophilus has been cocrystallized with either its cognate tRNAlys or Escherichia coli tRNAlys using ammonium sulfate as precipitant. The crystals grow from solutions containing a 1:2.5 stoichiometry of synthetase dimer to tRNA in 18-22% ammonium sulfate in 50 mM Tris-maleate buffer at pH 7.5. Both complexes form square prismatic, tetragonal crystals with very similar unit cell parameters (a = b = 233 A, c = 119 A) and diffract to at least 2.7 A resolution. However the homocomplex is of space group P42(1)2 and the heterocomplex of space group I422.
嗜热栖热菌的赖氨酰 - tRNA合成酶已分别与它的同源tRNAlys或大肠杆菌tRNAlys共结晶，使用硫酸铵作为沉淀剂。晶体在含有合成酶二聚体与tRNA化学计量比为1:2.5的溶液中生长，该溶液处于pH 7.5的50 mM Tris - 马来酸缓冲液中，硫酸铵浓度为18 - 22%。两种复合物均形成方形棱柱形的四方晶体，具有非常相似的晶胞参数（a = b = 233 Å，c = 119 Å），并且衍射分辨率至少为2.7 Å。然而，同源复合物属于空间群P42(1)2，异源复合物属于空间群I422。
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