ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Expression, purification and preliminary X-ray crystallographic analysis of Arf1-GDP in complex with dimeric p23 peptide.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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2 citing papers in PubMed, 5 citations in OpenAlex.
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5 authors at 3 institutions in 1 country.
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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 P6₁22, with unit-cell parameters a=b=80.6, c=336.0 Å, α=β=90, γ=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%.
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