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Cocrystallization of Lysyl–tRNA synthetase from Thermus thermophilus with its cognate tRNAlys and with Escherichia coli tRNAlys
Authors:A. D. Yaremchuk  S. Cusack  M. A. Tukalo  I. A. Krikliviy
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 Å, c = 119 Å) and diffract to at least 2.7 Å resolution. However the homocomplex is of space group P4212 and the heterocomplex of space group I422. © 1995 Wiley-Liss, Inc.
Keywords:lysyl-tRNA synthetase (Thermus thermophilus)  tRNAlys  crystallization  X-ray structure  aminoacyl-tRNA synthetase
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