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*

*この研究の対応する著者

研究成果: Article査読

1 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)332-335
ページ数4
ジャーナルActa Crystallographica Section F: Structural Biology and Crystallization Communications
69
3
DOI
出版ステータスPublished - 2013 3月
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 遺伝学
  • 凝縮系物理学

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