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°.

DOI: 10.1107/S1744309113026444

Cite this paper

@article{Lee2013CrystallizationAP, title={Crystallization and preliminary X-ray crystallographic studies of the CIDE-N domain of CIDE-3.}, author={Seung Mi Lee and Hyun Ho Park}, journal={Acta crystallographica. Section F, Structural biology and crystallization communications}, year={2013}, volume={69 Pt 11}, pages={1260-3} }