Crystallization and preliminary X-ray crystallographic analysis of yeast arginyl-tRNA synthetase-yeast tRNAArg complexes

被引:6
作者
Delagoutte, B
Keith, G
Moras, D
Cavarelli, J
机构
[1] ULP, INSERM, CNRS,UPR Biol Struct 9004, Inst Genet & Biol Mol & Cellulaire, F-67404 Illkirch Graffenstaden, France
[2] CNRS, Inst Biol Mol & Cellulaire, UPR Struct Macromol Biol & Mechanisms Reconnaissa, F-67084 Strasbourg, France
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2000年 / 56卷
关键词
D O I
10.1107/S0907444900001700
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Three different crystal forms of complexes between arginyl-tRNA synthetase from the yeast Saccharomyces cerevisae (yArgRS) and the yeast second major tRNA(Arg) (tRNA(ICG)(Arg)) 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 Angstrom 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, b = 107.47, c = 71.38 Angstrom. This crystal form presents the highest resolution obtained for an active form of an aminoacyl-tRNA synthetase-tRNA complex. The estimated V-m of 2.6 Angstrom(3) Da(-1) indicates one molecule of complex in the asymmetric unit. The three crystal forms were solved by the molecular-replacement method using the coordinates of the free yArgRS.
引用
收藏
页码:492 / 494
页数:3
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