Structure analysis of cytoplasmic dynein stalk domain

为了揭示动力蛋白对微管的识别机制，本研究对小鼠动力蛋白柄区的结晶条件进行了探索，获得了动力蛋白柄区的单晶。我制备了硒代蛋氨酸取代的蛋白质，并使用同步辐射（2.8 A分辨率）收集了晶体的衍射数据。用多波长反常色散（MAD）方法计算初始相位，得到蛋白质的部分模型（卷曲螺旋区）。该模型揭示了蛋氨酸的位置，这是通过使用硒的异常色散信号计算，移动那些报道的晶体结构。

In order to reveal the recognition mechanism of the microtubule by motor protein dynein, I have searched the crystallization condition of the mouse dynein stalk domain and could obtain single crystals. I prepared the selenomethionine-substituted protein and collected the diffraction data of the crystals using Synchrotron Radiation (2.8 A resolution). Initial phase are calculated by the multiwavelength anomalous dispersion (MAD) method, I could obtain the partial model of the protein (coiled-coil region). The model revealed that the positions of the methionine, which are calculated by using the anomalous dispersion signal of the selenium, are shifted those of the reported crystal structure.