Crystallization of threonyl-tRNA synthetase from Thermus thermophilus and preliminary crystallographic data.
Threonyl-tRNA synthetase from Thermus thermophilus (ttTRS) has been overproduced in Escherichia coli, purified and crystallized in solutions containing ammonium sulfate and glycerol. The crystals grew in the orthorhombic space group C222(1) with unit cell dimensions a = 119.5 A, b = 120.0 A, c = 317.5 A. The asymmetric unit is constituted of two monomers and the crystals contain 66% solvent. This paper reports the first crystals of ttTRS and preliminary crystallographic results since the presumed crystals of ttTRS described in a previous paper [1] were crystals of aspartyl-tRNA synthetase [2].
Cura
V
V
UPR 9004 de Biologie Structurale, IGBMC, CNRS/INSERM/ULP, Illkirch, France.
Kern
D
D
Mitschler
A
A
Moras
D
D
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli; D012995:Solubility; D013696:Temperature; D016963:Thermus thermophilus / Q000201:enzymology*; D013914:Threonine-tRNA Ligase / Q000737:chemistry* / Q000235:genetics
D013914:Threonine-tRNA Ligase