Cloning, expression, purification, crystallization and preliminary X-ray crystallographic investigations of a unique editing domain from archaebacteria.
Threonyl-tRNA synthetase (ThrRS) faces a crucial double-discrimination problem during the translation of genetic code. Most ThrRSs from the archaeal kingdom possess a unique editing domain that differs from those of eubacteria and eukaryotes. In order to understand the structural basis of the editing mechanism in archaea, the editing module of ThrRS from Pyrococcus abyssi comprising of the first 183 amino-acid residues was cloned, expressed, purified and crystallized. The crystals belong to the trigonal space group P3(1(2))21, with one molecule in the asymmetric unit.
Dwivedi
Shweta
S
Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India.
Kruparani
Shobha P
SP
Sankaranarayanan
Rajan
R
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D008970:Molecular Weight; D010957:Plasmids / Q000235:genetics; D019711:Pyrococcus / Q000737:chemistry* / Q000235:genetics*; D020133:Reverse Transcriptase Polymerase Chain Reaction; D013914:Threonine-tRNA Ligase / Q000737:chemistry* / Q000235:genetics
D013914:Threonine-tRNA Ligase