Crystallization and preliminary X-ray diffraction analysis of the tRNA-modification enzyme GidA from Aquifex aeolicus

Takuo Osawa, Hideko Inanaga, Tomoyuki Numata

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

The 5-carboxymethylaminomethyl modification of uridine at the first position of the tRNA anticodon is crucial for accurate protein synthesis by stabilizing the correct codon-anticodon pairing on the ribosome. Two conserved enzymes, GidA and MnmE, are involved in this modification process. Aquifex aeolicus GidA was crystallized in two different crystal forms: forms I and II. These crystals diffracted to 3.2 and 2.3 Å resolution, respectively, using synchrotron radiation at the Photon Factory. These crystals belonged to space groups I212121 and P21 with unit-cell parameters a = 101.6, b = 213.3, c = 231.7 Å and a = 119.4, b = 98.0, c = 129.6 Å, Β = 90.002°, respectively. The asymmetric units of these crystals are expected to contain two and four molecules, respectively.

Original languageEnglish
Pages (from-to)508-511
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume65
Issue number5
DOIs
Publication statusPublished - 2009

All Science Journal Classification (ASJC) codes

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

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