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Purification, crystallization and preliminary X-ray crystallographic studies of Drep2 CIDE domain.

ABSTRACT: Drep2 is a novel nuclease from the fruit fly that might have a similar function in apoptosis to DFF40 and DFF45, which are primary players in apoptotic DNA fragmentation. Drep2 contains a conserved CIDE domain of ?90 amino-acid residues that is involved in protein-protein interaction. In this study, the Drep2 CIDE domain was purified and crystallized by the hanging-drop vapour-diffusion method. X-ray diffraction data were then collected to a resolution of 2.3?Å. The crystals were found to belong to the orthorhombic space group P212121, with unit-cell parameters a = 50.28, b = 88.70, c = 113.37?Å.

SUBMITTER: Lee SM

PROVIDER: S-EPMC4188092 | biostudies-literature | 2014 Oct

REPOSITORIES: biostudies-literature

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Purification, crystallization and preliminary X-ray crystallographic studies of Drep2 CIDE domain.

Lee Seung Mi SM Park Hyun Ho HH

Acta crystallographica. Section F, Structural biology communications 20140925 Pt 10

Drep2 is a novel nuclease from the fruit fly that might have a similar function in apoptosis to DFF40 and DFF45, which are primary players in apoptotic DNA fragmentation. Drep2 contains a conserved CIDE domain of ∼90 amino-acid residues that is involved in protein-protein interaction. In this study, the Drep2 CIDE domain was purified and crystallized by the hanging-drop vapour-diffusion method. X-ray diffraction data were then collected to a resolution of 2.3 Å. The crystals were found to belong ...[more]

PMID: 25286952

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