Open AccessCrystallization and preliminary X‐ray crystallographic studies of the CIDE‐N domain of CIDE‐3
Author(s) -
Lee Seung Mi,
Park Hyun Ho
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113026444
Subject(s) - crystallization , crystallography , diffraction , chemistry , resolution (logic) , optics , physics , organic chemistry , artificial intelligence , computer science
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 P 3 2 , with unit‐cell parameters a = b = 63.35, c = 37.60 Å, γ = 120°.