With the advent of X-ray free-electron lasers (XFELs), new, high-throughput serial
crystallography techniques for macromolecular structure determination have emerged …

A new scientific frontier opened in 2009 with the start of operations of the world's first x-ray
free-electron laser (FEL), the Linac Coherent Light Source (LCLS), at SLAC National …

BACKGROUND Conformational changes are essential for the correct functioning of
biological macromolecules. Time-resolved x-ray crystallography extends an extremely …

Structure determination of proteins and other macromolecules has historically required the
growth of high-quality crystals sufficiently large to diffract x-rays efficiently while withstanding …

Serial femtosecond crystallography using ultrashort pulses from x-ray free electron lasers
(XFELs) enables studies of the light-triggered dynamics of biomolecules. We used …

Protein crystallography using synchrotron radiation sources has had a tremendous impact
on biology, having yielded the structures of thousands of proteins and given detailed insight …

In this review, we describe recent research developments into radiation damage effects in
macromolecular X-ray crystallography observed at synchrotrons and X-ray free electron …

X-ray free-electron lasers provide femtosecond-duration pulses of hard X-rays with a peak
brightness approximately one billion times greater than is available at synchrotron radiation …

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 …

The development and application of the free-electron X-ray laser (XFEL) to structure and
dynamics in biology since its inception in 2009 are reviewed. The research opportunities …