STRUCTURE OF CDC42HS IN COMPLEX W/ CATALYTIC DOMAIN OF CDC42GAP

我们的第一个实验是确定一个 电压门控钾通道的胞质结构域。 域 含有140种氨基酸，控制钾离子的门控， 负责心脏中的电传导的通道。 需要同步辐射是因为 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波长MAD实验中解决了该结构 在F2，数据为2.6
.这个结构直接导致了一个假设 对于域调节通道的门控的机制。 这一假设已通过功能研究进行了测试， 八个月以来的结构确定和文件正在进行 写着 我们的第二个实验是测定一种 完整的膜钾通道使用A1设施。 的 结构用MIR解析，数据为3.2
需要大量的 原生集和衍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.