X-ray diffraction has the potential to provide rich information about the protein conformational ensemble. Bragg diffraction is increasingly being used for ensemble modeling; however, Bragg analysis only reveals the mean charge density and cannot distinguish models that result from alternative collective motions. In contrast, diffuse scattering yields intensity between the Bragg peaks and reports on correlations in charge density variations. Diffuse scattering can be used to distinguish models with different atom displacement correlations and provides detailed information for validating ensemble models of crystalline proteins. Modern detectors, X-ray beamlines, and computational methods are bringing diffuse scattering data collection and modeling within reach for any crystallography lab. In addition, high-performance computing will enable real time data processing and models with increased accuracy.
Last modified: Tuesday, 18-Jul-2017 09:39:34 NZST
This page is maintained by the seminar list administrator.