嗜热栖热菌脯氨酰-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 Thermus thermophilus prolyl-tRNA synthetase.

作者信息

Yaremchuk A, Cusack S, Tukalo M

机构信息

EMBL Grenoble Outstation, 156X, 38042 Grenoble CEDEX 9, France.

出版信息

Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):195-6. doi: 10.1107/s0907444999015498.

DOI:10.1107/s0907444999015498

PMID:10666603

Abstract

Prolyl-tRNA synthetase from Thermus thermophilus (ProRSTT) was purified to homogeneity using a five-step purification procedure and was crystallized using ethylene glycol as a precipitant. Crystals of ProRSTT belong to the space group P2(1)2(1)2, with unit-cell parameters a = 132, b = 191, c = 125 A, have two homodimers per asymmetric unit and diffract to 2.4 A resolution. A complete native data set to 2.43 A resolution has been collected and a data set from ProRSTT in complex with proline has been collected to 2.9 A resolution.

摘要

嗜热栖热菌的脯氨酰 - tRNA合成酶（ProRSTT）通过五步纯化程序纯化至同质，并使用乙二醇作为沉淀剂进行结晶。ProRSTT的晶体属于空间群P2(1)2(1)2，晶胞参数a = 132、b = 191、c = 125 Å，每个不对称单元有两个同型二聚体，衍射分辨率为2.4 Å。已收集到分辨率为2.43 Å的完整天然数据集，并收集到ProRSTT与脯氨酸复合物的数据集，分辨率为2.9 Å。