Open AccessCrystallization and preliminary X‐ray analysis of peptidyl‐tRNA hydrolase from Thermus thermophilus HB8
Author(s) -
Matsumoto Ami,
Shimizu Yoshihiro,
Takemoto Chie,
Ueda Takuya,
Uchiumi Toshio,
Ito Kosuke
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113003424
Subject(s) - thermus thermophilus , transfer rna , hydrolase , orthorhombic crystal system , crystallization , chemistry , translation (biology) , stereochemistry , molecule , crystallography , crystal structure , enzyme , escherichia coli , biochemistry , rna , organic chemistry , messenger rna , gene
Peptidyl‐tRNA is produced from the ribosome as a result of aborted translation. Peptidyl‐tRNA hydrolase cleaves the ester bond between the peptide and the tRNA of peptidyl‐tRNA molecules, to recycle tRNA for further rounds of protein synthesis. In this study, peptidyl‐tRNA hydrolase from Thermus thermophilus HB8 (TthPth) was crystallized using 2‐methyl‐2,4‐pentanediol as a precipitant. The crystals belonged to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 47.45, b = 53.92, c = 58.67 Å, and diffracted X‐rays to atomic resolution (beyond 1.0 Å resolution). The asymmetric unit is expected to contain one TthPth molecule, with a solvent content of 27.13% ( V M = 1.69 Å 3 Da −1 ). The structure is being solved by molecular replacement.