Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl-tRNA synthetase.
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.
Bonnefond
Luc
L
Département Machineries Traductionnelles, Architecture et Réactivité de l'ARN, Université Louis Pasteur de Strasbourg, CNRS, IBMC, Strasbourg, France.
Frugier
Magali
M
Touzé
Elodie
E
Lorber
Bernard
B
Florentz
Catherine
C
Giegé
Richard
R
Rudinger-Thirion
Joëlle
J
Sauter
Claude
C
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*
D017931:DNA Primers; D014448:Tyrosine-tRNA Ligase