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Purification, crystallization and preliminary X-ray crystallographic studies of Drep2 CIDE domain
- Lee, Seung Mi;
- Park, Hyun Ho
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1초록
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 P212121, with unit-cell parameters a = 50.28, b = 88.70, c = 113.37 Å.
키워드
apoptosis; CIDE domain; DNA fragmentation factor; Drep2; Drosophila melanogaster; APOPTOTIC DNA FRAGMENTATION; CASPASE-ACTIVATED DNASE; PROTEIN; ICAD; INHIBITOR; COMPLEX; SYSTEM; MODE; FLY
- 제목
- Purification, crystallization and preliminary X-ray crystallographic studies of Drep2 CIDE domain
- 저자
- Lee, Seung Mi; Park, Hyun Ho
- 발행일
- 2014-10
- 유형
- Article
- 권
- 70
- 호
- 10
- 페이지
- 1414 ~ 1417
- 언어
- ENG
- 출판사
- INT UNION CRYSTALLOGRAPHY
- 발행국가
- 영국
- 분량
- 4 페이지
- ISSN
- E 2053-230X