title: Crystallization and preliminary X-ray crystallographic studies of Drep-3, a DFF-related protein from Drosophila melanogaster.
abstract: During apoptosis, DNA fragmentation is mainly mediated by the caspase-activated DFF40 nuclease. DFF40 exists as a heterodimeric complex with its inhibitor DFF45. Upon apoptosis induction, DFF45 is cleaved by caspases to allow DFF40 activation. Drep-3 is a recently identified regulator of the DFF40 system in Drosophila melanogaster. Here, Drep-3 was expressed with a C-terminal His tag in Escherichia coli and the protein was purified to homogeneity. Multi-angle light-scattering analysis showed that Drep-3 is a homotetramer in solution. Native and selenomethionine-substituted Drep-3 proteins were crystallized at 293 K and X-ray diffraction data were collected to 2.8 and 3.0 A resolution, respectively. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 56.9, b = 125.4, c = 168.7 A. The asymmetric unit is estimated to contain one homotetramer.
authors.affiliation: Department of Biochemistry, Weill Medical College and Graduate School of Medical Sciences of Cornell University, New York, NY 10021, USA.
authors.forename: Hyun Ho
authors.initials: HH
authors.lastname: Park
authors.forename: Hansel Emory
authors.initials: HE
authors.lastname: Tookes
authors.forename: Hao
authors.initials: H
authors.lastname: Wu
mesh_terms: D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D003851:Deoxyribonucleases / Q000737:chemistry; D029721:Drosophila Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000235:genetics; D006639:Histidine; D008027:Light; D012542:Scattering, Radiation; D012997:Solvents; D014961:X-Ray Diffraction
chemical_list: C402283:Drep3 protein, Drosophila; D029721:Drosophila Proteins; D012997:Solvents; D006639:Histidine; D003851:Deoxyribonucleases