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与甲酰甲硫氨酰 - tRNAfMet复合的大肠杆菌甲硫氨酰 - tRNAfMet甲酰转移酶的结晶及初步X射线分析。

Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNAMet(f) formyltransferase complexed with formyl-methionyl-tRNAMet(f).

作者信息

Schmitt E, Blanquet S, Mechulam Y

机构信息

Laboratoire de Biochimie, Unité Mixte de Recherche No. 7654 du Centre National de la Recherche Scientifique, Ecole Polytechnique, F-91128 Palaiseau CEDEX,

出版信息

Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):332-4. doi: 10.1107/S0907444998011780. Epub 1999 Jan 1.

DOI:10.1107/S0907444998011780
PMID:10089442
Abstract

The structure of methionyl-tRNAfMet(f) formyltransferase from E. coli, a monomeric protein of 34 kDa, has previously been determined at 2.0 A resolution. In the present work, this enzyme was crystallized as a complex with its macromolecular product, the initiator formyl-methionyl-tRNAfMet(f) (25 kDa). Polyethylene glycol 5000 monomethylether was used as a precipitating agent. The crystals are orthorhombic and have unit-cell parameters a = 201.7, b = 68.1, c = 86.4 A. They belong to space group P21212 and diffract to 2.8 A resolution. The structure is being solved with the help of a mercury derivative.

摘要

来自大肠杆菌的甲硫氨酰 - tRNAfMet(f)甲酰基转移酶是一种34 kDa的单体蛋白，其结构先前已在2.0 Å分辨率下确定。在本研究中，该酶与其大分子产物起始甲酰甲硫氨酰 - tRNAfMet(f)（25 kDa）形成复合物结晶。聚乙二醇5000单甲醚用作沉淀剂。晶体为正交晶系，晶胞参数a = 201.7、b = 68.1、c = 86.4 Å。它们属于空间群P21212，可衍射至2.8 Å分辨率。借助汞衍生物正在解析其结构。

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