Cocrystallization of lysyl-tRNA synthetase from Thermus thermophilus with its cognate tRNAlys and with Escherichia coli tRNAlys

Proteins
A YaremchukM Tukalo

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.

References

May 11, 1992·Nucleic Acids Research·K TamuraM Shimizu
Dec 1, 1990·Proceedings of the National Academy of Sciences of the United States of America·W H McClainJ Schneider
Jan 1, 1993·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·J Cavarelli, D Moras

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Citations

Oct 1, 1995·Nature Structural Biology·S Cusack
Aug 25, 2006·Journal of Biomolecular Structure & Dynamics·V R Chechetkin, V V Lobzin
Jun 8, 2001·Annual Review of Biochemistry·M V Rodnina, W Wintermeyer
Jul 23, 2013·PLoS Genetics·Jorge Fernández-VázquezElena Hidalgo
Feb 8, 2008·Virus Research·Truus E M Abbink, Ben Berkhout
Aug 1, 1995·Biological Chemistry Hoppe-Seyler·W Freist, D H Gauss

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