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Expression, purification and preliminary X-ray crystallographic analysis of Arf1-GDP in complex with dimeric p23 peptide.

ABSTRACT: Arf1 is a member of the Ras superfamily and is involved in COPI vesicle formation. Arf1-GDP can interact with dimeric p23. Here, human Arf1 (residues 18-181) was cloned, expressed and purified in Escherichia coli. For crystallization, Arf1-GDP was mixed with dimeric p23 peptide in a 1:5 molar ratio. Crystals were obtained which diffracted to 2.7?Å resolution. The crystals belonged to space group P6?22, with unit-cell parameters a=b=80.6, c=336.0?Å, ?=?=90, ?=120°. The asymmetric unit of the crystals contained two molecules, with a Matthews coefficient of 3.2?Å3?Da(-1) and a solvent content of 61.9%.

SUBMITTER: Zheng P

PROVIDER: S-EPMC3792679 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature

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Expression, purification and preliminary X-ray crystallographic analysis of Arf1-GDP in complex with dimeric p23 peptide.

Zheng Peng P Gao Feng F Deng Kai K Gong Weimin W Sun Zhe Z

Acta crystallographica. Section F, Structural biology and crystallization communications 20130928 Pt 10

Arf1 is a member of the Ras superfamily and is involved in COPI vesicle formation. Arf1-GDP can interact with dimeric p23. Here, human Arf1 (residues 18-181) was cloned, expressed and purified in Escherichia coli. For crystallization, Arf1-GDP was mixed with dimeric p23 peptide in a 1:5 molar ratio. Crystals were obtained which diffracted to 2.7 Å resolution. The crystals belonged to space group P6₁22, with unit-cell parameters a=b=80.6, c=336.0 Å, α=β=90, γ=120°. The asymmetric unit of the crys ...[more]

PMID: 24100571

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