STRUCTURAL STUDIES OF MEMBRANE PROTEINS

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 膜蛋白结构的确定仍然是结构生物学的前沿。衍射质量晶体的生长是一个瓶颈，而衍射到高分辨率的晶体生长是罕见的。使用一种新的策略，我们生长了四个完整的膜蛋白，这是目前在不同阶段的晶体学特征的晶体。一旦膜蛋白的晶体已经生长，筛选过程比可溶性蛋白更复杂。通常，在家用发电机上观察到的衍射很少，并且由于结晶条件的优化是基于衍射的反馈而不是晶体的视觉质量，因此需要更多的同步加速器时间来确定每个结构。

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. Membrane protein structure determination remains a frontier in structural biology. Growth of diffraction quality crystals is a bottleneck, while growth of crystals diffracting to high-resolution is rare. Using a new strategy, we grew crystals of four integral-membrane proteins, which are currently at different stages of crystallographic characterization. Once crystals of membrane proteins have been grown, the screening process is more involved than for soluble proteins. Often, little diffraction is observed at the home generator, and since the optimization of crystallization conditions is based on feedback from diffraction rather than from the visual quality of the crystals, much more synchrotron time is required to determine each structure.