Crystallization and preliminary X-ray crystallographic analysis of yeast arginyl-tRNA synthetase–yeast tRNAArg complexes - Archive ouverte HAL Access content directly
Journal Articles Acta Crystallographica Section D: Biological Crystallography Year : 2000

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

Abstract

Three different crystal forms of complexes between arginyl-tRNA synthetase from the yeast Saccharomyces cerevisae (yArgRS) and the yeast second major tRNAArg (tRNA^{\rm Arg}_{\rm 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 Å resolution at the European Synchrotron Radiation Facility ID14-4 beamline, belongs to the orthorhombic space group P21212, with unit-cell parameters a = 129.64, b = 107.47, c = 71.38 Å. This crystal form presents the highest resolution obtained for an active form of an aminoacyl-tRNA synthetase–tRNA complex. The estimated Vm of 2.6 Å3 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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hal-04087140 , version 1 (02-05-2023)

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Bénédicte Delagoutte, Gérard Keith, Dino Moras, Jean Cavarelli. Crystallization and preliminary X-ray crystallographic analysis of yeast arginyl-tRNA synthetase–yeast tRNAArg complexes. Acta Crystallographica Section D: Biological Crystallography, 2000, 56 (4), pp.492-494. ⟨10.1107/S0907444900001700⟩. ⟨hal-04087140⟩
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