Literature DB >> 10739930

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

B Delagoutte1, G Keith, D Moras, J Cavarelli.   

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.

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Year:  2000        PMID: 10739930     DOI: 10.1107/s0907444900001700

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

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

Authors:  B Delagoutte; D Moras; J Cavarelli
Journal:  EMBO J       Date:  2000-11-01       Impact factor: 11.598

  1 in total

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