TY - JOUR
T1 - X-ray diffraction analysis of a human tRNAGly acceptor-stem microhelix isoacceptor at 1.18 Å resolution
AU - Eichert, André
AU - Perbandt, Markus
AU - Schreiber, Angela
AU - Fürste, Jens P.
AU - Betzel, Christian
AU - Erdmann, Volker A.
AU - Förster, Charlotte
PY - 2009/1/28
Y1 - 2009/1/28
N2 - Interest has been focused on comparative X-ray structure analyses of different tRNAGly acceptor-stem helices. tRNAGly/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 tRNAGly 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 tRNAGly acceptor-stem microhelix with sequence 5′-G 1C2A3U4U5G 6G7-3′, 5′-C66C67A 68A69U70G71C72-3′ is reported. The crystals belonged to the monoclinic space group C2, 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.
AB - Interest has been focused on comparative X-ray structure analyses of different tRNAGly acceptor-stem helices. tRNAGly/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 tRNAGly 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 tRNAGly acceptor-stem microhelix with sequence 5′-G 1C2A3U4U5G 6G7-3′, 5′-C66C67A 68A69U70G71C72-3′ is reported. The crystals belonged to the monoclinic space group C2, 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.
UR - http://www.scopus.com/inward/record.url?scp=58549111413&partnerID=8YFLogxK
U2 - 10.1107/S1744309108040153
DO - 10.1107/S1744309108040153
M3 - Journal articles
C2 - 19153458
AN - SCOPUS:58549111413
SN - 1744-3091
VL - 65
SP - 59
EP - 62
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 1
ER -