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
Externally publishedYes

Fingerprint

Arsenate Reductases
arsenates
saccharomyces
His-His-His-His-His-His
Crystallization
X-Ray Diffraction
Yeast
X ray diffraction analysis
Saccharomyces cerevisiae
cdc25 Phosphatases
crystallization
proteins
genes
Crystals
Genes
Cell Cycle Checkpoints
diffraction
Recombinant Proteins
Sodium Chloride
crystals

ASJC Scopus subject areas

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

Cite this

Crystallization and preliminary X-ray diffraction analysis of Saccharomyces cerevisiae Ygr203p, a homologue of Acr2 arsenate reductase. / Moon, Jinho; Kim, Young Sil; Lee, Jae Young; Cho, Seung Je; Song, Hyun Kyu; Cho, Jong Hyun; Kim, B. Moon; Kim, Kyeong Kyu; Suh, Se Won.

In: Acta Crystallographica Section D: Biological Crystallography, Vol. 56, No. 6, 03.07.2000, p. 778-780.

Research output: Contribution to journalArticle

Moon, Jinho ; Kim, Young Sil ; Lee, Jae Young ; Cho, Seung Je ; Song, Hyun Kyu ; Cho, Jong Hyun ; Kim, B. Moon ; Kim, Kyeong Kyu ; Suh, Se Won. / Crystallization and preliminary X-ray diffraction analysis of Saccharomyces cerevisiae Ygr203p, a homologue of Acr2 arsenate reductase. In: Acta Crystallographica Section D: Biological Crystallography. 2000 ; Vol. 56, No. 6. pp. 778-780.
@article{3692b934764540339907448acf9e11c1,
title = "Crystallization and preliminary X-ray diffraction analysis of Saccharomyces cerevisiae Ygr203p, a homologue of Acr2 arsenate reductase",
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 {\AA}. The asymmetric unit contains a monomer, giving a crystal volume per protein mass (V(m)) of 2.61 {\AA}3 Da-1 and a solvent content of 53.8{\%}. The crystals diffract to better than 1.9 {\AA} resolution with Cu Kα X-rays. They are therefore suitable for high-resolution structure determination.",
author = "Jinho Moon and Kim, {Young Sil} and Lee, {Jae Young} and Cho, {Seung Je} and Song, {Hyun Kyu} and Cho, {Jong Hyun} and Kim, {B. Moon} and Kim, {Kyeong Kyu} and Suh, {Se Won}",
year = "2000",
month = "7",
day = "3",
doi = "10.1107/S0907444900005278",
language = "English",
volume = "56",
pages = "778--780",
journal = "Acta Crystallographica Section D: Structural Biology",
issn = "0907-4449",
publisher = "John Wiley and Sons Inc.",
number = "6",

}

TY - JOUR

T1 - Crystallization and preliminary X-ray diffraction analysis of Saccharomyces cerevisiae Ygr203p, a homologue of Acr2 arsenate reductase

AU - Moon, Jinho

AU - Kim, Young Sil

AU - Lee, Jae Young

AU - Cho, Seung Je

AU - Song, Hyun Kyu

AU - Cho, Jong Hyun

AU - Kim, B. Moon

AU - Kim, Kyeong Kyu

AU - Suh, Se Won

PY - 2000/7/3

Y1 - 2000/7/3

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0343133982&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0343133982&partnerID=8YFLogxK

U2 - 10.1107/S0907444900005278

DO - 10.1107/S0907444900005278

M3 - Article

VL - 56

SP - 778

EP - 780

JO - Acta Crystallographica Section D: Structural Biology

JF - Acta Crystallographica Section D: Structural Biology

SN - 0907-4449

IS - 6

ER -