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嗜热栖热菌苏氨酰-tRNA合成酶的结晶及初步晶体学数据

Crystallization of threonyl-tRNA synthetase from Thermus thermophilus and preliminary crystallographic data.

作者信息

Cura V, Kern D, Mitschler A, Moras D

机构信息

UPR 9004 de Biologie Structurale, IGBMC, CNRS/INSERM/ULP, Illkirch, France.

出版信息

FEBS Lett. 1995 Oct 23;374(1):110-2. doi: 10.1016/0014-5793(95)01089-w.

Abstract

Threonyl-tRNA synthetase from Thermus thermophilus (ttTRS) has been overproduced in Escherichia coli, purified and crystallized in solutions containing ammonium sulfate and glycerol. The crystals grew in the orthorhombic space group C222(1) with unit cell dimensions a = 119.5 A, b = 120.0 A, c = 317.5 A. The asymmetric unit is constituted of two monomers and the crystals contain 66% solvent. This paper reports the first crystals of ttTRS and preliminary crystallographic results since the presumed crystals of ttTRS described in a previous paper [1] were crystals of aspartyl-tRNA synthetase [2].

摘要

嗜热栖热菌的苏氨酰 - tRNA合成酶(ttTRS)已在大肠杆菌中过量表达,经纯化后在含有硫酸铵和甘油的溶液中结晶。晶体在正交空间群C222(1)中生长,晶胞参数为a = 119.5 Å,b = 120.0 Å,c = 317.5 Å。不对称单元由两个单体组成,晶体含有66%的溶剂。本文报道了ttTRS的首批晶体以及初步晶体学结果,因为之前一篇论文[1]中描述的推测的ttTRS晶体实际上是天冬氨酰 - tRNA合成酶的晶体[2]。

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