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

Ami Matsumoto, Yoshihiro Shimizu, Chie Takemoto, Takuya Ueda, Toshio Uchiumi, Kosuke Ito

Research output: Contribution to journalArticle

1 Citation (Scopus)

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 P212121, with unit-cell parameters a = 47.45, b = 53.92, c = 58.67Å, and diffracted X-rays to atomic resolution (beyond 1.0Å resolution). The asymmetric unit is expected to contain one TthPth molecule, with a solvent content of 27.13% (V M = 1.69Å3Da-1). The structure is being solved by molecular replacement.

Original languageEnglish
Pages (from-to)332-335
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume69
Issue number3
DOIs
Publication statusPublished - 2013 Mar

Keywords

  • Thermus thermophilus
  • peptidyl-tRNA hydrolase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

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