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Cocrystallization of Lysyl–tRNA synthetase from Thermus thermophilus with its cognate tRNA lys and with Escherichia coli tRNA lys
Author(s) -
Yaremchuk A. D.,
Cusack S.,
Tukalo M. A.,
Krikliviy I. A.
Publication year - 1995
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.340210309
Subject(s) - thermus thermophilus , transfer rna , escherichia coli , dimer , ammonium sulfate , space group , biology , stereochemistry , tetragonal crystal system , crystallography , chemistry , biochemistry , crystal structure , rna , x ray crystallography , organic chemistry , gene , physics , diffraction , optics
Lysyl‐tRNA synthetase from Thermus thermophilus has been cocrystallized with either its cognate tRNA lYS or Escherichia coli tRNA lys 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 P 42 1 2 and the heterocomplex of space group I 422. © 1995 Wiley‐Liss, Inc.