Open AccessTyrosyl‐tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl‐tRNA synthetase
Author(s) -
Bonnefond Luc,
Frugier Magali,
Touzé Elodie,
Lorber Bernard,
Florentz Catherine,
Giegé Richard,
Sauter Claude,
RudingerThirion Joëlle
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107012481
Subject(s) - crystallization , transfer rna , escherichia coli , tetragonal crystal system , tyrosine , resolution (logic) , crystallography , aminoacyl trna synthetase , biology , biochemistry , stereochemistry , chemistry , crystal structure , rna , gene , organic chemistry , artificial intelligence , computer science
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 Tyr charging, yielded crystals suitable for structure determination. These tetragonal crystals, belonging to space group P 4 3 2 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.