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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, ? = 120°.

SUBMITTER: Lee SM

PROVIDER: S-EPMC3818048 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic studies of the CIDE-N domain of CIDE-3.

Lee Seung Mi SM Park Hyun Ho HH

Acta crystallographica. Section F, Structural biology and crystallization communications 20131030 Pt 11

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 crysta ...[more]

PMID: 24192364

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