Preliminary Crystallographic Report
Cocrystallization of Lysyl–tRNA synthetase from Thermus thermophilus with its cognate tRNAlys and with Escherichia coli tRNAlys
Article first published online: 3 FEB 2004
Copyright © 1995 Wiley-Liss, Inc.
Proteins: Structure, Function, and Bioinformatics
Volume 21, Issue 3, pages 261–264, March 1995
How to Cite
Yaremchuk, A. D., Cusack, S., Tukalo, M. A. and Krikliviy, I. A. (1995), Cocrystallization of Lysyl–tRNA synthetase from Thermus thermophilus with its cognate tRNAlys and with Escherichia coli tRNAlys. Proteins, 21: 261–264. doi: 10.1002/prot.340210309
- Issue published online: 3 FEB 2004
- Article first published online: 3 FEB 2004
- Manuscript Accepted: 17 NOV 1994
- Manuscript Received: 16 NOV 1994
- lysyl-tRNA synthetase (Thermus thermophilus);
- X-ray structure;
- aminoacyl-tRNA synthetase
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.