Abstract
The
D. melanogaster
Drep-3 protein has been crystallized. Crystals were obtained at 293 K that diffracted to 2.8 Å resolution and belonged to space group
P
2
1
2
1
2
1
.
During apoptosis, DNA fragmentation is mainly mediated by the caspase-activated DFF40 nuclease. DFF40 exists as a heterodimeric complex with its inhibitor DFF45. Upon apoptosis induction, DFF45 is cleaved by caspases to allow DFF40 activation. Drep-3 is a recently identified regulator of the DFF40 system in
Drosophila melanogaster
. Here, Drep-3 was expressed with a C-terminal His tag in
Escherichia coli
and the protein was purified to homogeneity. Multi-angle light-scattering analysis showed that Drep-3 is a homotetramer in solution. Native and selenomethionine-substituted Drep-3 proteins were crystallized at 293 K and X-ray diffraction data were collected to 2.8 and 3.0 Å resolution, respectively. The crystals belong to space group
P
2
1
2
1
2
1
, with unit-cell parameters
a
= 56.9,
b
= 125.4,
c
= 168.7 Å. The asymmetric unit is estimated to contain one homotetramer.
