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

被引：1

作者：

Lee, Seung Mi

Park, Hyun Ho ^{[1
]}

机构：

[1] Yeungnam Univ, Sch Biotechnol, Gyongsan, South Korea

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2013年 / 69卷

基金：

新加坡国家研究基金会;

关键词：

CHAPERONE ACTIVITY; PROTEIN COMPLEXES; CRYSTAL-STRUCTURE; CELL-DEATH; APOPTOSIS; DFF40; FSP27; OBESITY;

D O I：

10.1107/S1744309113026444

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

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 similar to 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 angstrom. The crystals were found to belong to space group P3(2), with unit-cell parameters a = b = 63.35, c = 37.60 angstrom, gamma = 120 degrees.

引用

收藏

页码：1260 / 1263

页数：4

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