STRUCTURE OF CDC42HS IN COMPLEX W/ CATALYTIC DOMAIN OF CDC42GAP

我们的第一个实验是确定一个化合物的结构 来自电压门控钾通道的细胞质结构域。域名 含有140个氨基酸，控制着钾的门控 负责心脏电传导的通道。 需要同步辐射是因为它的微观尺寸 晶体(50微米)和由于严重的非同构 重原子衍生化。含硒蛋氨酸的蛋白质 并在3个波长的MAD实验中进行了求解 在F2，数据为2.6。这种结构直接导致了一种假设 用于域调节通道选通的机制。 这一假说已经通过功能研究对 结构确定已经八个月了，一篇论文正在 写的。我们的第二个实验是一个结构的确定 使用A1设施的整体膜钾通道。这个 结构由MIR求解，数据为3.2并且需要大量的 本机集和派生集的数据收集会话。这 结构构成了我们目前对钾的理解的基础 离子通道的选择性。4.

Our first experiment was the structure determination of a cytoplasmic domain from a voltage-gated potassium channel. The domain contains 140 amino acids and controls the gating of a potassium channel that is responsible for electrical conduction in the heart. Synchrotron radiation was required because of the microscopic size of the crystals (50 microns) and because of severe nonisomorphism upon heavy atom derivitization. Protein containing selenomethionine was produced and the structure was solved in a 3 wavelength MAD experiment at F2 with data to 2.6
. The structure directly led to a hypothesis for the mechanism by which the domain regulates gating of the channel. The hypothesis has been tested through functional studies over the eight months since the structure determination and a paper is being written. Our second experiment was the structure determination of an integral membrane potassium channel using the A1 facility. The structure was solved by MIR with data to 3.2
and required numerous data collection sessions for both native and derivative sets. This structure forms the basis for our current understanding of potassium selectivity in ion channels. 4.