Open AccessHuman tRNA Gly acceptor‐stem microhelix: crystallization and preliminary X‐ray diffraction analysis at 1.2 Å resolution
Author(s) -
Förster Charlotte,
Szkaradkiewicz Karol,
Perbandt Markus,
Brauer Arnd B. E.,
Borowski Tordis,
Fürste Jens P.,
Betzel Christian,
Erdmann Volker A.
Publication year - 2007
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309107041528
Subject(s) - transfer rna , resolution (logic) , crystallization , crystallography , biology , stereochemistry , chemistry , rna , genetics , gene , organic chemistry , artificial intelligence , computer science
The major dissimilarities between the eukaryotic/archaebacterial‐type and eubacterial‐type glycyl‐tRNA synthetase systems (GlyRS; class II aminoacyl‐tRNA synthetases) represent an intriguing example of evolutionarily divergent solutions to similar biological functions. The differences in the identity elements of the respective tRNA Gly systems are located within the acceptor stem and include the discriminator base U73. In the present work, the human tRNA Gly acceptor‐stem microhelix was crystallized in an attempt to analyze the structural features that govern the correct recognition of tRNA Gly by the eukaryotic/archaebacterial‐type glycyl‐tRNA synthetase. The crystals of the human tRNA Gly acceptor‐stem helix belong to the monoclinic space group C 2, with unit‐cell parameters a = 37.12, b = 37.49, c = 30.38 Å, α = γ = 90, β = 113.02°, and contain one molecule per asymmetric unit. A high‐resolution data set was acquired using synchrotron radiation and the data were processed to 1.2 Å resolution.