title: 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.
authors.affiliation: Department of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
authors.forename: Seung Mi
authors.initials: SM
authors.lastname: Lee
authors.affiliation: Department of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
authors.forename: Hyun Ho
authors.initials: HH
authors.lastname: Park
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D029721:Drosophila Proteins / Q000737:chemistry* / Q000302:isolation & purification; D004331:Drosophila melanogaster / Q000201:enzymology*; D008969:Molecular Sequence Data; D054730:Protein Interaction Domains and Motifs
chemical_list: C402282:Drep2 protein, Drosophila; D029721:Drosophila Proteins
keywords: CIDE domain; DNA fragmentation factor; Drep2; Drosophila melanogaster; apoptosis