title: Crystallization and preliminary X-ray crystallographic studies of the CIDE-N domain of CIDE-3.
abstract: The CIDE-3 protein plays a critical role in lipid metabolism by its involvement in lipid droplet formation. CIDE-3 contains two conserved cell-death-inducing DFF45-like effector (CIDE) domains (CIDE-N at the N-terminus and CIDE-C at the C-terminus) of ∼90 amino-acid residues that are involved in protein-protein interaction. In this study, the CIDE-N domain of CIDE-3 was purified and crystallized by the hanging-drop vapour-diffusion method and X-ray diffraction data were collected from the crystals to a resolution of 2.0 Å. The crystals were found to belong to space group P3(2), with unit-cell parameters a = b = 63.35, c = 37.60 Å, γ = 120°.
authors.affiliation: School of Biotechnology and Graduate School of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
authors.forename: Seung Mi
authors.initials: SM
authors.lastname: Lee
authors.forename: Hyun Ho
authors.initials: HH
authors.lastname: Park
mesh_terms: D000818:Animals; D002850:Chromatography, Gel; D003460:Crystallization; D018360:Crystallography, X-Ray; D051379:Mice; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins; C525805:fat-specific protein 27, mouse
keywords: CIDE domain; CIDE-3; DNA fragmentation factor; apoptosis; lipid metabolism