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Title: Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl-tRNA synthetase

Abstract

Crystals of human mitochondrial tyrosyl-tRNA synthetase lacking the C-terminal S4-like domain diffract to 2.7 Å resolution and are suitable for structure determination. Human mitochondrial tyrosyl-tRNA synthetase and a truncated version with its C-terminal S4-like domain deleted were purified and crystallized. Only the truncated version, which is active in tyrosine activation and Escherichia coli tRNA{sup Tyr} charging, yielded crystals suitable for structure determination. These tetragonal crystals, belonging to space group P4{sub 3}2{sub 1}2, were obtained in the presence of PEG 4000 as a crystallizing agent and diffracted X-rays to 2.7 Å resolution. Complete data sets could be collected and led to structure solution by molecular replacement.

Authors:
; ; ; ; ; ; ;  [1]
  1. Département ‘Machineries Traductionnelles’, Architecture et Réactivité de l’ARN, Université Louis Pasteur de Strasbourg, CNRS, IBMC, 15 Rue René Descartes, 67084 Strasbourg (France)
Publication Date:
OSTI Identifier:
22360303
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 63; Journal Issue: Pt 4; Other Information: PMCID: PMC2330213; PMID: 17401211; PUBLISHER-ID: hc5025; OAI: oai:pubmedcentral.nih.gov:2330213; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; ESCHERICHIA COLI; MATHEMATICAL SOLUTIONS; RESOLUTION; SOLUTIONS; SPACE GROUPS

Citation Formats

Bonnefond, Luc, Frugier, Magali, Touzé, Elodie, Lorber, Bernard, Florentz, Catherine, Giegé, Richard, E-mail: r.giege@ibmc.u-strasbg.fr, Rudinger-Thirion, Joëlle, and Sauter, Claude. Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl-tRNA synthetase. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107012481.
Bonnefond, Luc, Frugier, Magali, Touzé, Elodie, Lorber, Bernard, Florentz, Catherine, Giegé, Richard, E-mail: r.giege@ibmc.u-strasbg.fr, Rudinger-Thirion, Joëlle, & Sauter, Claude. Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl-tRNA synthetase. United Kingdom. doi:10.1107/S1744309107012481.
Bonnefond, Luc, Frugier, Magali, Touzé, Elodie, Lorber, Bernard, Florentz, Catherine, Giegé, Richard, E-mail: r.giege@ibmc.u-strasbg.fr, Rudinger-Thirion, Joëlle, and Sauter, Claude. Sun . "Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl-tRNA synthetase". United Kingdom. doi:10.1107/S1744309107012481.
@article{osti_22360303,
title = {Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl-tRNA synthetase},
author = {Bonnefond, Luc and Frugier, Magali and Touzé, Elodie and Lorber, Bernard and Florentz, Catherine and Giegé, Richard, E-mail: r.giege@ibmc.u-strasbg.fr and Rudinger-Thirion, Joëlle and Sauter, Claude},
abstractNote = {Crystals of human mitochondrial tyrosyl-tRNA synthetase lacking the C-terminal S4-like domain diffract to 2.7 Å resolution and are suitable for structure determination. Human mitochondrial tyrosyl-tRNA synthetase and a truncated version with its C-terminal S4-like domain deleted were purified and crystallized. Only the truncated version, which is active in tyrosine activation and Escherichia coli tRNA{sup Tyr} charging, yielded crystals suitable for structure determination. These tetragonal crystals, belonging to space group P4{sub 3}2{sub 1}2, were obtained in the presence of PEG 4000 as a crystallizing agent and diffracted X-rays to 2.7 Å resolution. Complete data sets could be collected and led to structure solution by molecular replacement.},
doi = {10.1107/S1744309107012481},
journal = {Acta Crystallographica. Section F},
number = Pt 4,
volume = 63,
place = {United Kingdom},
year = {Sun Apr 01 00:00:00 EDT 2007},
month = {Sun Apr 01 00:00:00 EDT 2007}
}