Park Hyun Ho
Department of Biochemistry, Yeungnam University, Gyeongsan, Republic of Korea.
Acta Crystallogr F Struct Biol Commun. 2017 Aug 1;73(Pt 8):481-485. doi: 10.1107/S2053230X1701069X. Epub 2017 Jul 26.
DREP4 is a nuclease from fruit fly that is involved in apoptotic DNA fragmentation. DREP4 contains a conserved CIDE domain that acts as a protein-interaction module and is critical for its function. In this study, it was found that DREP4 CIDE domains form filament-like structures in solution. The length of the highly ordered filament-like structure is dependent on the salt concentration. By adjusting the salt concentration the DREP4 CIDE domain could be crystallized, and X-ray diffraction data were collected to a resolution of 1.9 Å. The crystals were found to belong to the orthorhombic space group P222, with unit-cell parameters a = 53.08, b = 76.58, c = 174.59 Å.
DREP4是一种来自果蝇的核酸酶,参与凋亡性DNA片段化过程。DREP4含有一个保守的CIDE结构域,该结构域作为蛋白质相互作用模块,对其功能至关重要。在本研究中,发现DREP4 CIDE结构域在溶液中形成丝状结构。高度有序的丝状结构的长度取决于盐浓度。通过调节盐浓度,DREP4 CIDE结构域可以结晶,并收集到分辨率为1.9 Å的X射线衍射数据。发现这些晶体属于正交空间群P222,晶胞参数为a = 53.08,b = 76.58,c = 174.59 Å。