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

Title
Crystallization and preliminary X-ray crystallographic studies of the CIDE-N domain of CIDE-3
Author(s)
박현호이승미
Keywords
CHAPERONE ACTIVITY; PROTEIN COMPLEXES; CRYSTAL-STRUCTURE; CELL-DEATH; APOPTOSIS; DFF40; FSP27; OBESITY
Issue Date
201311
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.69, pp.1260 - 1263
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 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.
URI
http://hdl.handle.net/YU.REPOSITORY/28579http://dx.doi.org/10.1107/S1744309113026444
ISSN
1744-3091
Appears in Collections:
이과대학 > 화학생화학부 > Articles
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML


qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE