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

Research output: Contribution to journalArticle

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 Jul 3

ASJC Scopus subject areas

  • Structural Biology

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