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 …

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 …

X-ray crystallography at X-ray free-electron laser sources is a powerful method for studying
macromolecules at biologically relevant temperatures. Moreover, when combined with …

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 …

The high peak brilliance and femtosecond pulse duration of X-ray free-electron lasers
(XFELs) provide new scientific opportunities for experiments in physics, chemistry and …

X-ray free electron lasers (XFELs) have the potential to revolutionize macromolecular
structural biology due to the unique combination of spatial coherence, extreme peak …

We report a method for serial X-ray crystallography at X-ray free-electron lasers (XFELs),
which allows for full use of the current 120-Hz repetition rate of the Linear Coherent Light …

Highly efficient data-collection methods are required for successful macromolecular
crystallography (MX) experiments at X-ray free-electron lasers (XFELs). XFEL beamtime is …

The Coherent X-ray Imaging (CXI) instrument specializes in hard X-ray, in-vacuum, high
power density experiments in all areas of science. Two main sample chambers, one …