[Isolation and crystallization of phenylalanyl-tRNA-synthetase from Thermus thermophilus HB8].
Method of isolation of phenylalanyl-tRNA synthetase from Thermus thermophilus HB8 is described, including chromatography on DEAE-sepharose, ammonium sulfate fractionation, hydrofobic chromatography on Toyopearl, gel filtration on ultrogel AcA-34, chromatography on phenylalanylaminohexyl-sepharose and heparine-sepharose. Yield of the purified enzyme was 10 mg from 1 kg of T. thermophilus cells. The enzyme is found to consist of two types of subunits with molecular masses 92 and 36 kDa and is likely to be a tetramer protein with molecular mass 250 kDa. Crystals of phenylalanyl-tRNA synthetase suitable for X-ray structural studies have been obtained.
D000604:Amino Acyl-tRNA Synthetases / Q000302:isolation & purification*; D003460:Crystallization; D010652:Phenylalanine-tRNA Ligase / Q000302:isolation & purification*; D013824:Thermus / Q000201:enzymology*
D000604:Amino Acyl-tRNA Synthetases; D010652:Phenylalanine-tRNA Ligase
Vydelenie i kristallizatsiia fenilalanil-tRNK-sintetazy iz Thermus thermophilus HB8.