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Drep2 CIDE结构域的纯化、结晶及初步X射线晶体学研究。

Purification, crystallization and preliminary X-ray crystallographic studies of Drep2 CIDE domain.

作者信息

Lee Seung Mi, Park Hyun Ho

机构信息

Department of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.

出版信息

Acta Crystallogr F Struct Biol Commun. 2014 Oct;70(Pt 10):1414-7. doi: 10.1107/S2053230X14019165. Epub 2014 Sep 25.

Abstract

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.

摘要

Drep2是一种来自果蝇的新型核酸酶,在细胞凋亡中可能具有与DFF40和DFF45类似的功能,而DFF40和DFF45是细胞凋亡过程中DNA片段化的主要参与者。Drep2包含一个约90个氨基酸残基的保守CIDE结构域,该结构域参与蛋白质-蛋白质相互作用。在本研究中,通过悬滴气相扩散法对Drep2 CIDE结构域进行了纯化和结晶。随后收集了分辨率为2.3 Å的X射线衍射数据。发现晶体属于正交空间群P212121,晶胞参数a = 50.28,b = 88.70,c = 113.37 Å。

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