Cocrystallization of lysyl-tRNA synthetase from Thermus thermophilus with its cognate tRNAlys and with Escherichia coli tRNAlys.
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.
Yaremchuk
A D
AD
European Molecular Biology Laboratory, Grenoble Outstation, France.
Krikliviy
I A
IA
Cusack
S
S
Tukalo
M A
MA
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
D012329:RNA, Bacterial; D012357:RNA, Transfer, Lys; D008250:Lysine-tRNA Ligase