Purification, crystallization and preliminary X-ray crystallographic studies of Drep2 CIDE domain
2014 ◽
Vol 70
(10)
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pp. 1414-1417
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Keyword(s):
X Ray
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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.
1999 ◽
Vol 55
(6)
◽
pp. 1231-1233
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2014 ◽
Vol 70
(11)
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pp. 1560-1562
2016 ◽
Vol 72
(6)
◽
pp. 480-484
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2017 ◽
Vol 73
(8)
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pp. 481-485