Structure analysis of cytoplasmic dynein stalk domain

为了揭示运动蛋白动力蛋白对微管的识别机制，我搜索了小鼠动力蛋白柄结构域的结晶条件，可以获得单晶。制备了硒代蛋氨酸取代蛋白，并用同步辐射（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）法计算初始相位，得到蛋白质的部分模型（螺旋区）。该模型表明，利用硒的异常色散信号计算的蛋氨酸的位置与报道的晶体结构的位置发生了移位。

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.