Macromolecular crystallography at synchrotron sources has proven to be the most influential
method within structural biology, producing thousands of structures since its inception. While …

In 1999, researchers extended X-ray crystallography to allow the imaging of noncrystalline
specimens by measuring the X-ray diffraction pattern of a noncrystalline specimen and then …

X-ray crystallography provides the vast majority of macromolecular structures, but the
success of the method relies on growing crystals of sufficient size. In conventional …

This article describes the software suite GROMACS (Groningen MAchine for Chemical
Simulation) that was developed at the University of Groningen, The Netherlands, in the early …

X-ray free-electron lasers have opened up the possibility of structure determination of
protein crystals at room temperature, free of radiation damage. The femtosecond-duration …

X-ray free-electron lasers have enabled new approaches to the structural determination of
protein crystals that are too small or radiation-sensitive for conventional analysis. For …

We introduce the EMC algorithm for reconstructing a particle's three-dimensional (3D)
diffraction intensity from very many photon shot-noise limited two-dimensional …

X-ray free-electron lasers (XFELs) enable crystallographic structure determination beyond
the limitations imposed upon synchrotron measurements by radiation damage. The need for …

X-ray free-electron lasers (FELs) are promising tools for structural determination of
macromolecules via coherent x-ray scattering. During ultrashort and ultraintense x-ray …

We present the first single-shot images of ferromagnetic, nanoscale spin order taken with
femtosecond x-ray pulses. X-ray-induced electron and spin dynamics can be outrun with …