Peptidyl-tRNA hydrolase (Pth) cleaves the ester bond between the peptide and the tRNA of peptidyl-tRNA molecules, which are the product of aborted translation. In the present work, Pth from Escherichia coli was crystallized with the acceptor-TC domain of tRNA using 1,4-butanediol as a precipitant. The crystals belonged to the hexagonal space group P61, with unit-cell parameters a = b = 55.1, c = 413.1 Å, and diffracted X-rays beyond 2.4 Å resolution. The asymmetric unit is expected to contain two complexes of Pth and the acceptor-TC domain of tRNA (V M = 2.8 Å 3 Da -1), with a solvent content of 60.8%. The structure is being solved by molecular replacement.
|ジャーナル||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|出版ステータス||Published - 2011 12 1|
ASJC Scopus subject areas
- Structural Biology
- Condensed Matter Physics