DIFFRACTION ANOMALOUS FINE STRUCTURE (DAFS) FOR PROTEINS

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。 本项目的目的是确定利用蛋白质晶体进行衍射异常精细结构(DAFS)实验的可行性。在测试是否可以使用DAFS观察到与EXAFS实验相同的短程结构信息以及与XANES实验相同的结构和光谱灵敏度的初始方法中，使用P6肌红蛋白晶体在Fe K吸收边以4 eV的能量阶跃收集了10度的衍射数据。数据分析正在进行中。从这些初步实验中可以明显看出，DAFS实验可以受益于在Blu-Ice中开发特定的数据收集脚本或特定的数据收集图形用户界面。在未来，我们计划使用DAFS来同时研究同一元素中占据不同位置的两个原子。

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. The goal of this project is to determine the feasibility of Diffraction Anomalous Fine Structure (DAFS) experiments with protein crystals. In initial approaches to test if the equivalent short range structural information as an EXAFS experiment and the same structural and spectroscopic sensitivity as an XANES experiment may be observed using DAFS, 10 degrees of diffraction data were collected at 4 eV steps in energy across the Fe K-absorption edge using a crystal of P6 myoglobin. Data analysis is underway. From these initial experiments, it was evident that DAFS experiments could benefit from the development of specific data collection scripts or a specific data collection GUI in Blu-Ice. In the future, we plan to use DAFS to simultaneously study two atoms of the same element which occupy nonequivalent sites in a crystal.