Purification, crystallization and preliminary X-ray crystallographic studies of Drep2 CIDE domain
Copyright policy )Purification, crystallization and preliminary X-ray crystallographic studies of Drep2 CIDE domain
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 groupP212121, with unit-cell parametersa= 50.28,b= 88.70,c= 113.37 Å.
- Yeungnam University Korea (Republic of)
Drosophila melanogaster, Molecular Sequence Data, Chromatography, Gel, Animals, Drosophila Proteins, Protein Interaction Domains and Motifs, Amino Acid Sequence, Crystallization, Crystallography, X-Ray
Drosophila melanogaster, Molecular Sequence Data, Chromatography, Gel, Animals, Drosophila Proteins, Protein Interaction Domains and Motifs, Amino Acid Sequence, Crystallization, Crystallography, X-Ray
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