Crystallization and preliminary X-ray crystallographic study of alanyl-tRNA synthetase from the archaeon Archaeoglobus fulgidus

Ryuya Fukunaga, Shigeyuki Yokoyama

Research output: Contribution to journalArticlepeer-review

Abstract

In order to analyze the alanyl-tRNA synthetase from the archaeon Archaeoglobus fulgidus, the N-terminal fragment lacking the dimerization domain and the C-terminal dimerization-domain fragment were each overexpressed in Escherichia coli, purified and crystallized. A 3.7 Å resolution data set was collected for the N-terminal fragment. The crystal belongs to the tetragonal space group P41 or P43, with unit-cell parameters a = b = 101.15, c = 124.24 Å. For the C-terminal fragment, a SeMet MAD data set was collected to 3.2 Å resolution. The crystal belongs to the orthorhombic space group P2221, with unit-cell parameters a = 124.15, b = 131.91, c = 138.68 Å.

Original languageEnglish (US)
Pages (from-to)224-228
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume63
Issue number3
DOIs
StatePublished - Feb 13 2007
Externally publishedYes

Keywords

  • AlaRS
  • Alanine
  • Archaeoglobus fulgidus
  • Dimerization
  • Editing
  • tRNa

ASJC Scopus subject areas

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

Fingerprint

Dive into the research topics of 'Crystallization and preliminary X-ray crystallographic study of alanyl-tRNA synthetase from the archaeon Archaeoglobus fulgidus'. Together they form a unique fingerprint.

Cite this