Abstract
We provide a historical introduction spanning the past 50 years of synchrotron radiation protein crystallography. We then provide a resume of current trends. These help us to celebrate the huge influence that synchrotron radiation, and now X-ray lasers, has had on the scope of protein crystallography. It has also accelerated the development of closely allied methods such as neutron protein crystallography, which has adopted the synchrotron Laue method as its own as well as developing monochromatic and time-of-flight methods. Also, the democratic access to central synchrotron facility beamlines has prompted similarly operated centres of electron cryo-microscopy and micro-electron diffraction. We offer our thoughts on the current trends across this scientific landscape.