@article{,
title = {Crystallization and preliminary X-ray crystallographic analysis of yeast arginyl-tRNA synthetase-yeast tRNAArg complexes},
author = { B. Delagoutte and G. Keith and D. Moras and J. Cavarelli},
year = {2000},
date = {2000-01-01},
journal = {Acta Crystallogr D Biol Crystallogr},
volume = {56},
number = {Pt 4},
pages = {492-4},
abstract = {Three different crystal forms of complexes between arginyl-tRNA synthetase from the yeast Saccharomyces cerevisae (yArgRS) and the yeast second major tRNA(Arg) (tRNA(Arg)(ICG)) isoacceptor have been crystallized by the hanging-drop vapour-diffusion method in the presence of ammonium sulfate. Crystal form II, which diffracts beyond 2.2 A resolution at the European Synchrotron Radiation Facility ID14-4 beamline, belongs to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 129.64},
note = {0907-4449
Journal Article},
keywords = {&, Arg/*chemistry/isolation, Arginine-tRNA, cerevisiae/enzymology/genetics, Crystallization, Crystallography, Fungal/chemistry/isolation, Gov't, Ligase/*chemistry/isolation, Non-U.S., purification/*metabolism, purification/metabolism, RNA, Saccharomyces, Support, Transfer, X-Ray},
pubstate = {published},
tppubtype = {article}
}
Three different crystal forms of complexes between arginyl-tRNA synthetase from the yeast Saccharomyces cerevisae (yArgRS) and the yeast second major tRNA(Arg) (tRNA(Arg)(ICG)) isoacceptor have been crystallized by the hanging-drop vapour-diffusion method in the presence of ammonium sulfate. Crystal form II, which diffracts beyond 2.2 A resolution at the European Synchrotron Radiation Facility ID14-4 beamline, belongs to the orthorhombic space group P2(1)2(1)2, with unit-cell parameters a = 129.64