title: Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl-tRNA synthetase.
abstract: 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 P4(3)2(1)2, were obtained in the presence of PEG 4000 as a crystallizing agent and diffracted X-rays to 2.7 A resolution. Complete data sets could be collected and led to structure solution by molecular replacement.
authors.affiliation: Département Machineries Traductionnelles, Architecture et Réactivité de l'ARN, Université Louis Pasteur de Strasbourg, CNRS, IBMC, Strasbourg, France.
authors.forename: Luc
authors.initials: L
authors.lastname: Bonnefond
authors.forename: Magali
authors.initials: M
authors.lastname: Frugier
authors.forename: Elodie
authors.initials: E
authors.lastname: Touzé
authors.forename: Bernard
authors.initials: B
authors.lastname: Lorber
authors.forename: Catherine
authors.initials: C
authors.lastname: Florentz
authors.forename: Richard
authors.initials: R
authors.lastname: Giegé
authors.forename: Joëlle
authors.initials: J
authors.lastname: Rudinger-Thirion
authors.forename: Claude
authors.initials: C
authors.lastname: Sauter
mesh_terms: D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D006801:Humans; D008928:Mitochondria / Q000201:enzymology*; D011487:Protein Conformation; D014448:Tyrosine-tRNA Ligase / Q000737:chemistry*
chemical_list: D017931:DNA Primers; D014448:Tyrosine-tRNA Ligase