Purification, crystallization and preliminary X-ray crystallographic studies of Drep2 CIDE domain

Title
Purification, crystallization and preliminary X-ray crystallographic studies of Drep2 CIDE domain
Author(s)
박현호이승미
Keywords
APOPTOTIC DNA FRAGMENTATION; CASPASE-ACTIVATED DNASE; PROTEIN; ICAD; INHIBITOR; COMPLEX; SYSTEM; MODE; FLY
Issue Date
201410
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.70, pp.1414 - 1417
Abstract
Drep2 is a novel nuclease from the fruit fly that might have a similar function in apoptosis to DFF40 and DFF45, which are primary players in apoptotic DNA fragmentation. Drep2 contains a conserved CIDE domain of similar to 90 amino-acid residues that is involved in protein-protein interaction. In this study, the Drep2 CIDE domain was purified and crystallized by the hanging-drop vapour-diffusion method. X-ray diffraction data were then collected to a resolution of 2.3 angstrom. The crystals were found to belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 50.28, b = 88.70, c = 113.37 angstrom.
URI
http://hdl.handle.net/YU.REPOSITORY/30675http://dx.doi.org/10.1107/S2053230X14019165
ISSN
1744-3091
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이과대학 > 화학생화학부 > Articles
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