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X‐ray diffraction analysis of a human tRNA Gly acceptor‐stem microhelix isoacceptor at 1.18 Å resolution
Author(s) -
Eichert André,
Perbandt Markus,
Schreiber Angela,
Fürste Jens P.,
Betzel Christian,
Erdmann Volker A.,
Förster Charlotte
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309108040153
Subject(s) - transfer rna , resolution (logic) , crystallography , x ray crystallography , biology , diffraction , chemistry , genetics , rna , physics , gene , optics , artificial intelligence , computer science
Interest has been focused on comparative X‐ray structure analyses of different tRNA Gly acceptor‐stem helices. tRNA Gly /glycyl‐tRNA synthetase belongs to the so‐called class II system, in which the tRNA identity elements consist of simple and unique determinants that are located in the tRNA acceptor stem and the discriminator base. Comparative structure investigations of tRNA Gly microhelices provide insight into the role of tRNA identity elements. Predominant differences in the structures of glycyl‐tRNA synthetases and in the tRNA identity elements between prokaryotes and eukaryotes point to divergence during the evolutionary process. Here, the crystallization and high‐resolution X‐ray diffraction analysis of a human tRNA Gly acceptor‐stem microhelix with sequence 5′‐G 1 C 2 A 3 U 4 U 5 G 6 G 7 ‐3′, 5′‐C 66 C 67 A 68 A 69 U 70 G 71 C 72 ‐3′ is reported. The crystals belonged to the monoclinic space group C 2, with unit‐cell parameters a = 37.32, b = 37.61, c = 30.47 Å, β = 112.60° and one molecule per asymmetric unit. A data set was collected using synchrotron radiation and data were processed within the resolution range 50.0–1.18 Å. The structure was solved by molecular replacement.

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