X-ray crystallographic analysis of an ABC transporter

了解ABC蛋白的作用机制和开发靶向ABC蛋白的新治疗策略将大大加速三维结构。从单细胞真核生物的出口型ABC转运蛋白的晶体结构确定的多波长异常色散（MAD）方法使用的X射线衍射数据测量在SPring-8。在这项研究中获得的分辨率是最好的真核生物ABC蛋白迄今为止报道。

Understanding the mechanism of action of ABC proteins and developing new therapeutic strategies that target ABC proteins would be considerably accelerated with the three-dimensional structures. Crystal structure of an exporter-type ABC transporter from a unicellular eukaryote was determined by the multiwavelength anomalous dispersion(MAD) method using the X-ray diffraction data measured at SPring-8. The resolution obtained in this study is best among those of eukaryotic ABC proteins ever reported to date.