STRUCTURE DETERMINATION OF A MEMBRANE PROTEIN USING SULFUR SAD

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 一种胞外膜蛋白不能结合Se和其他重原子来确定结构。开发了一种收集S数据进行结构确定的策略(S K边位于5.015 A)。数据记录在波长2 A处，加入氦冷流以减少背景散射。收集高度冗余的数据，产生22个冗余(晶体上的3个位置，每个360度数据，总共1080度)，产生10%到2.1A分辨率的RSYM。使用1个图像的楔形(每0.5度)以逆光束模式收集图像。振荡，Phi旋转180度)。将对数据进行分析，以确定该方法的结构和相关性。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. An extracellular membrane protein failed to incorporate Se and other heavy atoms for structure determination. A strategy was developed to collect S data for structure determination (the S K-edge is at 5.015 A). Data were recorded at a wavelength of 2 A. A helium cold stream was incorporated to reduce background scatter. Highly redundant data were collected yielding a redundancy of 22 (3 positions on the crystal, 360 degrees of data each, 1080 degrees total) yielding an Rsym of 10% to 2.1 A resolution. Images were collected in an inverse beam mode using a wedge of 1 image (for every 0.5 deg. oscillation, phi was rotated 180 degrees). The data will be analyzed to establish the structure and the relevance of the method.