Crystallization and preliminary X-ray analysis of peptidyl-tRNA hydrolase from Escherichia coli in complex with the acceptor-TC domain of tRNA

Kosuke Ito, Hao Qi, Yoshihiro Shimizu, Ryo Murakami, Kin Ichiro Miura, Takuya Ueda, Toshio Uchiumi

研究成果: Article査読

8 被引用数 (Scopus)

抄録

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 from Escherichia coli was crystallized with the acceptor-TC domain of tRNA using 1,4-butanediol as a precipitant. The crystals belonged to the hexagonal space group P61, with unit-cell parameters a = 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-TC domain of tRNA (V M = 2.8 Å 3 Da -1), with a solvent content of 60.8%. The structure is being solved by molecular replacement.

本文言語English
ページ(範囲)1566-1569
ページ数4
ジャーナルActa Crystallographica Section F: Structural Biology and Crystallization Communications
67
12
DOI
出版ステータスPublished - 2011 12 1
外部発表はい

ASJC Scopus subject areas

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

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