SMALL ANGLE X-RAY SCATTERING STUDIES ON ACTIN BUNDLES

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。子项目及 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。 从scruin的旋转半径的扩展或变化，我们将测量N-和C-末端β-螺旋桨域与旋转半径扩展之间的距离范围。由于scruin控制着顶体束中的肌动蛋白扭曲，因此这些结构域的相对位置将给出可以储存在肌动蛋白扭曲中的应变的上限。我们先前已经收集了溶液散射数据来测量Rg作为pCa的函数。然而，我们无法提取Rg中的可变性以达到我们所需的精度。通过对探测器的改进，我们可以重新收集数据并提取测量值。

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. From the spread or variability in the radius of gyration of scruin, we will measure the range in distances that separate the N-and C-terminal beta-propeller domains from the spread in the radius of gyration. Because scruin controls actin twist in the acrosomal bundle, the relative positions of the domains will give an upper boundry on the strain that can be stored in the twist of actin. We have previously collected solution scattering data to measure the Rg as a function of pCa. However, we cannot extract the variability in the Rg to the accuracy that we need. With improvements to the detector, we can re-collect the data and extract the measurements.