Radiation damage remains a fundamental limitation to the success of X-ray macromolecular crystallography (MX) experiments. The program RADDOSE-3D [1,2] estimates the dose absorbed by samples during data collection at synchrotron sources, allowing direct comparison of radiation damage between experiments carried out with different samples and beam parameters. Here, I present a number of...
One of the key opportunities offered by the development of x-ray free-electron lasers is the determination, at atomic resolution, of the three-dimensional structure of biologically relevant macromolecules. The basic idea underlying molecular imaging using x-ray free-electron lasers is the ``diffract-and-destroy'' concept: If one uses an x-ray pulse that is sufficiently short (on the order of...
X-ray spectroscopy probes the electronic structure around an analyte element in a sample. The electronic structure relates to the formal oxidation and spin state and the atomic structure around the analyte element. The sensitivity to small modification of the electronic structure makes X-ray spectroscopy strongly responsive to small changes of the sample due to X-ray irradiation. Thus, X-ray...
Size-exclusion chromatography small-angle X-ray solution scattering (SEC-SAXS) has become a standard method for modern bio-SAXS synchrotron light sources (Ryan et al. 2018; Brennich et al. 2016; Blanchet et al. 2015). However, the contamination of data by radiation damage remains a major issue resulting in poor post-processing of SEC-SAXS data. Several statistical tools have been developed to...
During small angle X-ray scattering studies of proteins in solutions, radiation damages may occur during exposure to the synchrotron radiation, which most often involves the protein aggregation process, but global conformational changes such as the domain swapping phenomenon is also possible.
The domain swapping phenomenon has been known for several decades and has been identified in numerous...
