Open AccessCrystallization and preliminary X‐ray diffraction analysis of an Escherichia coli tRNA Gly acceptor‐stem microhelix
Author(s) -
Förster Charlotte,
Perbandt Markus,
Brauer Arnd B. E.,
Brode Svenja,
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/s1744309106052870
Subject(s) - transfer rna , aminoacylation , escherichia coli , crystallization , resolution (logic) , base pair , biology , crystallography , stereochemistry , chemistry , genetics , dna , rna , organic chemistry , artificial intelligence , gene , computer science
The tRNA Gly and glycyl‐tRNA synthetase (GlyRS) system is an evolutionary special case within the class II aminoacyl‐tRNA synthetases because two divergent types of GlyRS exist: an archaebacterial/human type and an eubacterial type. The tRNA identity elements which determine the correct aminoacylation process are located in the aminoacyl domain of tRNA Gly . To obtain further insight concerning structural investigation of the identity elements, the Escherichia coli seven‐base‐pair tRNA Gly acceptor‐stem helix was crystallized. Data were collected to 2.0 Å resolution using synchrotron radiation. Crystals belong to space group P 3 1 21 or P 3 2 21, with unit‐cell parameters a = b = 35.35, c = 130.82 Å, α = β = 90, γ = 120° and two molecules in the asymmetric unit.