Crystallographic analysis relies on the scattering of quanta from arrays of atoms that
populate a repeating lattice. While large crystals built of lattices that appear ideal are sought …

The development of single-photon-counting detectors, such as the PILATUS, has been a
major recent breakthrough in macromolecular crystallography, enabling noise-free detection …

Next-generation synchrotron radiation sources, such as X-ray free-electron lasers, energy
recovery linacs, and ultra-low-emittance storage rings, are catalyzing novel methods of …

Single-particle imaging (SPI) with X-ray free-electron lasers has the potential to change
fundamentally how biomacromolecules are imaged. The structure would be derived from …

Prompted by methodological advances in measurements with X-ray free electron lasers, it
was realized in the last two years that traditional (or conventional) methods for data …

An outstanding question in X-ray single particle imaging experiments has been the
feasibility of imaging sub 10-nm-sized biomolecules under realistic experimental conditions …

Serial synchrotron-based crystallography using intense microfocused X-ray beams, fast-
framing detectors and protein microcrystals held at 300 K promises to expand the range of …

Essentially all the steps of the crystallographic process have undergone a tremendous
transformation in the last 10–20 years, and the progress has changed completely the way …

The intense X-ray pulses from free-electron lasers, of only femtoseconds duration, outrun
most of the processes that lead to structural degradation in X-ray exposures of …

Serial crystallography (SX) has become an established technique for protein structure
determination, especially when dealing with small or radiation-sensitive crystals and …