STRUCTURAL ANALYSIS OF RUVC RESOLVASE & ITS DNA SUBSTRATE

RuvC是已知的唯一能分解四向DNA的内切酶 建筑群更为人所知的是霍利迪交界处。X射线结晶学 研究表明，RuvC的活性部位在拓扑上类似于 HIV-1等其他多核苷酸转移酶的催化结构域 整合酶、核糖核酸酶H和MUA。我们报道了成功的结晶 四种序列特异性RuvC-Holliday连接复合体及其相互作用 溴和碘的衍生物。这些晶体络合物的衍射率 2.8E分辨率与常规震源。同步辐射 将极大地促进在两种情况下确定这些结构 方法：高分辨率反射将显示更高的强度 Sigma值，并且高度准直的光束将减少 漫射散射。

RuvC is the only known endonuclease to resolve the four-way DNA complex better known as the Holliday junction. X-ray crystallographic studies reveal the active site of RuvC is topologically similar to the catalytic domain of other polynucleotidyl transferases such as HIV-1 Integrase, RNAse H and MuA. We report the successful crystallization of four sequence specific RuvC-Holliday junction complexes and their Bromine and Iodine derivatives. These crystal complexes diffract to 2.8 E resolution with conventional sources. Synchrotron radiation will greatly facilitate the determination of these structures in two ways: high resolution reflections will show greater intensity over sigma values, and the highly collimated beam will decrease the amount of diffuse scattering.