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Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB8.

ABSTRACT: 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 P2?2?2?, 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% (VM=1.69?Å3?Da(-1)). The structure is being solved by molecular replacement.

SUBMITTER: Matsumoto A

PROVIDER: S-EPMC3606586 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Thermus thermophilus HB8.

Matsumoto Ami A Shimizu Yoshihiro Y Takemoto Chie C Ueda Takuya T Uchiumi Toshio T Ito Kosuke K

Acta crystallographica. Section F, Structural biology and crystallization communications 20130227 Pt 3

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 P2₁2₁2₁, with unit-cell parameters a=47.45, b=53.92, c=58 ...[more]

PMID: 23519816

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