Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli CyaY, a structural homologue of human frataxin

Myong Gyong Lee, Seung Je Cho, Jin Kuk Yang, Hyun Kyu Song, Se Won Suh

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

CyaY is a 106-residue protein from Escherichia coli. It shows aminoacid sequence similarity to human frataxin and a frataxin homologue in Saccharomyces cerevisiae, Yfh1p. The former is associated with the disease Friedreich ataxia and the latter plays a key role in iron homeostasis in mitochondria. CyaY has been overexpressed in soluble form in E. coli. The recombinant protein with a His 6 tag at its C-terminus has been crystallized at 296 K using polyethylene glycol (PEG) 4000 as a precipitant. Native diffraction data have been collected to 1.8 Å using Cu Kα X-rays. The crystals belong to the trigonal space group P3 121 (or P3 221), with unit-cell parameters a = b = 44.66, c = 99.87 Å, α = β = 90.0, γ= 120.0°. The asymmetric unit contains one molecule of recombinant CyaY, with a corresponding V(m) of 2.13 Å 3 Da -1 and solvent content of 42.3%.

Original languageEnglish
Pages (from-to)920-921
Number of pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number7
DOIs
Publication statusPublished - 2000 Jul 26
Externally publishedYes

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ASJC Scopus subject areas

  • Clinical Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biophysics
  • Condensed Matter Physics
  • Structural Biology

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