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Purification, crystallization and preliminary X‐ray crystallographic studies of Drep2 CIDE domain
Author(s) -
Lee Seung Mi,
Park Hyun Ho
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14019165
Subject(s) - orthorhombic crystal system , crystallography , crystallization , dna fragmentation , apoptosis , nuclease , chemistry , dna , biology , microbiology and biotechnology , crystal structure , biochemistry , programmed cell death , organic chemistry
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 ∼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 Å. The crystals were found to belong to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 50.28, b = 88.70, c = 113.37 Å.