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

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 …

In order to address the specific needs of the emerging technique ofserial femtosecond
crystallography', in which structural information is obtained from small crystals illuminated by …

CrystFEL is a suite of programs for processing data fromserial crystallography'experiments,
which are usually performed using X-ray free-electron lasers (FELs) but also increasingly …

Photosynthesis, a process catalysed by plants, algae and cyanobacteria converts sunlight to
energy thus sustaining all higher life on Earth. Two large membrane protein complexes …

High-intensity femtosecond pulses from an X-ray free-electron laser enable pump–probe
experiments for the investigation of electronic and nuclear changes during light-induced …

The Trypanosoma brucei cysteine protease cathepsin B (TbCatB), which is involved in host
protein degradation, is a promising target to develop new treatments against slee** …

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 …