title: Cocrystallization of lysyl-tRNA synthetase from Thermus thermophilus with its cognate tRNAlys and with Escherichia coli tRNAlys.
abstract: Lysyl-tRNA synthetase from Thermus thermophilus has been cocrystallized with either its cognate tRNAlys or Escherichia coli tRNAlys using ammonium sulfate as precipitant. The crystals grow from solutions containing a 1:2.5 stoichiometry of synthetase dimer to tRNA in 18-22% ammonium sulfate in 50 mM Tris-maleate buffer at pH 7.5. Both complexes form square prismatic, tetragonal crystals with very similar unit cell parameters (a = b = 233 A, c = 119 A) and diffract to at least 2.7 A resolution. However the homocomplex is of space group P42(1)2 and the heterocomplex of space group I422.
authors.affiliation: European Molecular Biology Laboratory, Grenoble Outstation, France.
authors.forename: A D
authors.initials: AD
authors.lastname: Yaremchuk
authors.forename: I A
authors.initials: IA
authors.lastname: Krikliviy
authors.forename: S
authors.initials: S
authors.lastname: Cusack
authors.forename: M A
authors.initials: MA
authors.lastname: Tukalo
mesh_terms: D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics*; D008250:Lysine-tRNA Ligase / Q000737:chemistry*; D012329:RNA, Bacterial / Q000737:chemistry; D012357:RNA, Transfer, Lys / Q000737:chemistry*; D013696:Temperature; D016963:Thermus thermophilus / Q000201:enzymology* / Q000235:genetics*; D013997:Time Factors
chemical_list: D012329:RNA, Bacterial; D012357:RNA, Transfer, Lys; D008250:Lysine-tRNA Ligase