Synchrotron-based protein crystallography continues to accelerate, driven by new and upgraded high-brightness sources, improved optics, faster large-area detectors, robust automation and streamlined data handling. These advances are making increasingly challenging structural biology projects feasible and are reshaping how synchrotron experiments integrate with today’s wider structural biology methods. While AI models are now routinely used in molecular replacement software for macromolecular crystal structure determination, synchrotron experimental methods remain vital for detailed model refinement, and even validating AI models. Also extracting key chemical information, with anomalous dispersion at tuneable beamlines still playing an important role especially in identifying metals and other such atoms in proteins.
This special issue in Journal of Synchrotron Radiation, edited by John R. Helliwell and Marian Szebenyi, and their Overview with Colin Nave, with a Perspective from Keith Hodgson, as well as articles from a majority of the facilities worldwide, explores the evolving landscape in depth. It also highlights the expanding impact of fragment screening and binding studies (from cryogenic up to body temperatures) and the rapidly developing frontiers of time-resolved and serial crystallography. In particular, the issue charts the synergy between XFEL-based serial femtosecond crystallography and serial synchrotron crystallography, culminating in recent demonstrations of microsecond time resolution at upgraded synchrotrons such as ESRF–EBS, pointing to a future where synchrotrons and X-ray lasers together enable ever more powerful studies of biological structure, dynamics and function.
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Image Credit:
Phillips, J.C., Wlodawer, A., Yevitz, M.M. and Hodgson, K.O., 1976. Applications of synchrotron radiation to protein crystallography: preliminary results. Proceedings of the National Academy of Sciences, 73(1), pp.128-132.
Rosenbaum, G., Holmes, K.C. and Witz, J., 1971. Synchrotron radiation as a source for X-ray diffraction. Nature, 230(5294), pp.434-437.
