Cloning, expression, purification, crystallization and preliminary X-ray crystallographic investigations of a unique editing domain from archaebacteria

Dwivedi, S. ; Kruparani, S. P. ; Sankaranarayanan, R. (2004) Cloning, expression, purification, crystallization and preliminary X-ray crystallographic investigations of a unique editing domain from archaebacteria Acta Crystallographica Section D, 60 . pp. 1662-1664. ISSN 0907-4449

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Official URL: http://scripts.iucr.org/cgi-bin/paper?bw5054

Related URL: http://dx.doi.org/10.1107/S0907444904017329

Abstract

Threonyl-tRNA synthetase (ThrRS) faces a crucial double-discrimination problem during the translation of genetic code. Most ThrRSs from the archaeal kingdom possess a unique editing domain that differs from those of eubacteria and eukaryotes. In order to understand the structural basis of the editing mechanism in archaea, the editing module of ThrRS from Pyrococcus abyssi comprising of the first 183 amino-acid residues was cloned, expressed, purified and crystallized. The crystals belong to the trigonal space group P31(2)21, with one molecule in the asymmetric unit.

Item Type:Article
Source:Copyright of this article belongs to International Union of Crystallography.
Keywords:Editing Domains; Threonyl-tRNA Synthetase
ID Code:66865
Deposited On:28 Oct 2011 04:02
Last Modified:28 Oct 2011 04:02

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