The International Year of Crystallography saw the number of macromolecular structures
deposited in the Protein Data Bank cross the 100000 mark, with more than 90000 of these …

Proteins that contain metal cofactors are expected to be highly radiation sensitive since the
degree of X-ray absorption correlates with the presence of high-atomic-number elements …

Radiation damage induced by X-ray beams during macromolecular diffraction experiments
remains an issue of concern in structural biology. While advances in our understanding of …

Single particle imaging at x-ray free electron lasers (XFELs) has the potential to determine
the structure and dynamics of single biomolecules at room temperature. Two major hurdles …

The bright ultrafast pulses of X-ray Free-Electron Lasers allow investigation into the structure
of matter under extreme conditions. We have used single pulses to ionize and probe water …

We describe a method to compute photon–matter interaction and atomic dynamics with x-ray
lasers using a hybrid code based on classical molecular dynamics and collisional-radiative …

The prospect of single particle imaging with atomic resolution is one of the scientific drivers
for the development of X-ray free-electron lasers. The assumption since the beginning has …

The development of X-ray free-electron lasers (XFELs) has opened the possibility to
investigate the ultrafast dynamics of biomacromolecules using X-ray diffraction. Whereas an …

Over the last decade X-ray free-electron laser (XFEL) sources have been made available to
the scientific community. One of the most successful uses of these new machines has been …

X-ray free-electron lasers (XFELs) have a unique capability for time-resolved studies of
protein dynamics and conformational changes on femto-and pico-second time scales. The …