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Crystallization and Preliminary X-ray Crystallographic Analysis of Yeast Arginyl-tRNA Synthetase-yeast TRNAArg Complexes

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Specialty Chemistry
Date 2000 Mar 31
PMID 10739930
Citations 1
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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, b = 107.47, c = 71. 38 A. 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 A(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.

Citing Articles

tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding.

Delagoutte B, Moras D, Cavarelli J EMBO J. 2000; 19(21):5599-610.

PMID: 11060012 PMC: 305789. DOI: 10.1093/emboj/19.21.5599.