用同步辐射装置收集了Sau3AI的C端蛋白晶体在se吸收边附近三个波长下的衍射数据,通过多波长反常散射(Multi-wavelength Anomalous Dispersion,MAD)法解决了晶体的衍射相位问题,解析了Sau3AI的c端蛋白的结构。结果表明,Sau3AI-C的结构与DNA错配修复蛋白MutH相似,结构中间的凹槽是Sau3AI-C与DNA的潜在结合区域。
The Multi-wavelength Anomalous Dispersion (MAD) method is an important method for three- dimensional structure determination of protein crystals. Diffraction datasets of the C-terminal fragment of Sau3AI crystal were collected at three different wavelengths. The structure of Sau3AI-C was solved by MAD method. It shows that this structure is similar to DNA mismatch repair protein MutH. Structural analysis indicates that the cleft in the middle of the structure is the potential binding site for DNA.