Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase fromEscherichia coliin complex with the acceptor-TΨC domain of tRNA

Abstract

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 fromEscherichia coliwas crystallized with the acceptor-TΨC domain of tRNA using 1,4-butanediol as a precipitant. The crystals belonged to the hexagonal space groupP61, with unit-cell parametersa = 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-TΨC domain of tRNA (VM= 2.8 Å3 Da−1), with a solvent content of 60.8%. The structure is being solved by molecular replacement.