Purification, crystallization and preliminary X-ray diffraction analysis of a cystathionine β-synthase domain-containing protein, CDCP2, from Arabidopsis thaliana

Byung Cheon Jeong, Kyoung Shin Yoo, Kwang Wook Jung, Jeong Sheop Shin, Hyun Kyu Song

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Cystathione β-synthase domain-containing protein 2 (CDCP2) from Arabidopsis thaliana has been overexpressed and purified to homogeneity. As an initial step towards three-dimensional structure determination, crystals of recombinant CDCP2 protein have been obtained using polyethylene glycol 8000 as a precipitant. The crystals diffracted to 2.4 Å resolution using synchrotron radiation and belonged to the trigonal space group P3 121 or P3 221, with unit-cell parameters a = b = 56.360, c = 82.596 Å, α = β = 90, γ = 120°. The asymmetric unit contains one CDCP2 molecule and the solvent content is approximately 41%.

Original languageEnglish
Pages (from-to)825-827
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume64
Issue number9
DOIs
Publication statusPublished - 2008 Sep 11

Fingerprint

Cystathionine
Arabidopsis Proteins
Crystallization
purification
X-Ray Diffraction
X ray diffraction analysis
Purification
crystallization
proteins
Synchrotrons
diffraction
Proteins
x rays
Radiation
Crystals
Synchrotron radiation
crystals
homogeneity
glycols
polyethylenes

ASJC Scopus subject areas

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

Cite this

@article{47f5b3020d174e9ebfd1a204948b4b92,
title = "Purification, crystallization and preliminary X-ray diffraction analysis of a cystathionine β-synthase domain-containing protein, CDCP2, from Arabidopsis thaliana",
abstract = "Cystathione β-synthase domain-containing protein 2 (CDCP2) from Arabidopsis thaliana has been overexpressed and purified to homogeneity. As an initial step towards three-dimensional structure determination, crystals of recombinant CDCP2 protein have been obtained using polyethylene glycol 8000 as a precipitant. The crystals diffracted to 2.4 {\AA} resolution using synchrotron radiation and belonged to the trigonal space group P3 121 or P3 221, with unit-cell parameters a = b = 56.360, c = 82.596 {\AA}, α = β = 90, γ = 120°. The asymmetric unit contains one CDCP2 molecule and the solvent content is approximately 41{\%}.",
author = "Jeong, {Byung Cheon} and Yoo, {Kyoung Shin} and Jung, {Kwang Wook} and Shin, {Jeong Sheop} and Song, {Hyun Kyu}",
year = "2008",
month = "9",
day = "11",
doi = "10.1107/S1744309108025128",
language = "English",
volume = "64",
pages = "825--827",
journal = "Acta Crystallographica Section F:Structural Biology Communications",
issn = "1744-3091",
publisher = "John Wiley and Sons Ltd",
number = "9",

}

TY - JOUR

T1 - Purification, crystallization and preliminary X-ray diffraction analysis of a cystathionine β-synthase domain-containing protein, CDCP2, from Arabidopsis thaliana

AU - Jeong, Byung Cheon

AU - Yoo, Kyoung Shin

AU - Jung, Kwang Wook

AU - Shin, Jeong Sheop

AU - Song, Hyun Kyu

PY - 2008/9/11

Y1 - 2008/9/11

N2 - Cystathione β-synthase domain-containing protein 2 (CDCP2) from Arabidopsis thaliana has been overexpressed and purified to homogeneity. As an initial step towards three-dimensional structure determination, crystals of recombinant CDCP2 protein have been obtained using polyethylene glycol 8000 as a precipitant. The crystals diffracted to 2.4 Å resolution using synchrotron radiation and belonged to the trigonal space group P3 121 or P3 221, with unit-cell parameters a = b = 56.360, c = 82.596 Å, α = β = 90, γ = 120°. The asymmetric unit contains one CDCP2 molecule and the solvent content is approximately 41%.

AB - Cystathione β-synthase domain-containing protein 2 (CDCP2) from Arabidopsis thaliana has been overexpressed and purified to homogeneity. As an initial step towards three-dimensional structure determination, crystals of recombinant CDCP2 protein have been obtained using polyethylene glycol 8000 as a precipitant. The crystals diffracted to 2.4 Å resolution using synchrotron radiation and belonged to the trigonal space group P3 121 or P3 221, with unit-cell parameters a = b = 56.360, c = 82.596 Å, α = β = 90, γ = 120°. The asymmetric unit contains one CDCP2 molecule and the solvent content is approximately 41%.

UR - http://www.scopus.com/inward/record.url?scp=51149099574&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=51149099574&partnerID=8YFLogxK

U2 - 10.1107/S1744309108025128

DO - 10.1107/S1744309108025128

M3 - Article

VL - 64

SP - 825

EP - 827

JO - Acta Crystallographica Section F:Structural Biology Communications

JF - Acta Crystallographica Section F:Structural Biology Communications

SN - 1744-3091

IS - 9

ER -