Crystallization and preliminary X-ray diffraction analysis of Saccharomyces cerevisiae Ygr203p, a homologue of Acr2 arsenate reductase

  • Jinho Moon
  • , Young Sil Kim
  • , Jae Young Lee
  • , Seung Je Cho
  • , Hyun Kyu Song
  • , Jong Hyun Cho
  • , B. Moon Kim
  • , Kyeong Kyu Kim
  • , Se Won Suh*
  • *Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

Ygr203p, a 148-residue protein encoded by the ygr203w gene of Saccharomyces cerevisiae, is a homologue of the yeast Acr2 arsenate reductase encoded by the acr2 (or ypr200c) gene. It also shows significant sequence similarity to the human cell-cycle control Cdc25 phosphatase family. It has been overexpressed in soluble form in Escherichia coli with a His6 tag at its C-terminus. The recombinant protein has been crystallized at 296 K using sodium chloride as precipitant. The crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 40.48, b = 50.95, c = 91.95 Å. The asymmetric unit contains a monomer, giving a crystal volume per protein mass (V(m)) of 2.61 Å3 Da-1 and a solvent content of 53.8%. The crystals diffract to better than 1.9 Å resolution with Cu Kα X-rays. They are therefore suitable for high-resolution structure determination.

Original languageEnglish
Pages (from-to)778-780
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number6
DOIs
Publication statusPublished - 2000
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology

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