STRUCTURAL ANALYSIS OF RUVC RESOLVASE & ITS DNA SUBSTRATE

RuvC是目前已知的唯一一种能分解四向DNA的核酸内切酶 被称为霍利迪枢纽的建筑群 x射线晶体学 研究表明RuvC的活性位点在拓扑结构上与 其他多核苷酸转移酶如HIV-1的催化结构域 整合酶、RNA酶H和MuA。 我们报告成功的结晶 四种序列特异性RuvC-Holliday连接复合物及其 溴和碘的衍生物。 这些晶体复合物可用于 2.8 E分辨率与传统来源。 同步辐射 这将大大有助于确定这些结构在两个 方式：高分辨率反射将显示更大的强度， sigma值，并且高度准直的光束将减少 漫散射

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.