Yaremchuk A D, Cusack S, Aberg A, Gudzera O, Kryklivyi I, Tukalo M
European Molecular Biology Laboratory, Grenoble Outstation, France.
Proteins. 1995 Aug;22(4):426-8. doi: 10.1002/prot.340220413.
Histidyl-tRNA synthetase (HisRS) has been purified from the extreme thermophile Thermus thermophilus. The protein has been crystallized separately with histidine and with its cognate tRNAHis. Both crystals have been obtained using the vapor diffusion method with ammonium sulphate as precipitant. The crystals of HisRS with histidine belong to the spacegroup P2(1)2(1)2 with cell parameters a = 171.3 A, b = 214.7 A, c = 49.3 A, alpha = beta = gamma = 90 degrees. A complete data set to a resolution of 2.7A with an Rmerge on intensities of 4.1% has been collected on a single frozen crystal. A partial data set collected on a crystal of HisRS in complex with tRNAHis shows that the crystals are tetragonal with cell parameters a = b = 232 A, c = 559 A, alpha = beta = gamma = 90 degrees and diffract to about 4.5 A resolution.
组氨酰 - tRNA合成酶（HisRS）已从嗜热栖热菌（Thermus thermophilus）中纯化出来。该蛋白质已分别与组氨酸及其同源tRNAHis结晶。两种晶体均采用硫酸铵作为沉淀剂的气相扩散法获得。HisRS与组氨酸形成的晶体属于空间群P2(1)2(1)2，晶胞参数为a = 171.3 Å，b = 214.7 Å，c = 49.3 Å，α = β = γ = 90°。在一块冷冻晶体上收集到了完整数据集，分辨率为2.7 Å，强度的合并R值为4.1%。在与tRNAHis形成复合物的HisRS晶体上收集的部分数据集表明，这些晶体为四方晶系，晶胞参数为a = b = 232 Å，c = 559 Å，α = β = γ = 90°，衍射分辨率约为4.5 Å。
