X-Ray Free Electron Laser (XFEL) Service
Biological macromolecules are the basis of all life activities, and their structure and functional studies have been a major frontier topic in life science research. X-ray crystallography is the most important method to study the three-dimensional structures of biological macromolecules. Currently, nearly 89% of the protein structures in the Protein Data Bank are obtained by synchrotron X-ray sources, but the radiation damage of X-rays limits the application of X-ray crystallography in protein structure and dynamics studies.
X-ray free-electron lasers (xfel) use free electrons as a medium to generate X-ray pulses with very high peak intensities and ultra-short pulse durations to break the link between radiation damage, sample size, and resolution, which passes through the sample before the X-ray damage. XFEL can obtain high-resolution protein structures and electronic state information. It can be used for both protein nanocrystals and giant virus particles, providing new opportunities for protein structure and dynamics studies.
