The use of high-brilliance synchrotron radiation is indispensible for the structural investigation of biological structure from the atomic scale determination of macromolecules to phase-contrast imaging of macroscopic tissue and even whole organisms. The methods to determine structure all utilize the coherent scattering of X-rays from the sample. These methods include macromolecular crystallography (MX), small-angle X-ray scattering (SAXS) and X-ray microscopy (XM). The impact of synchrotron radiation on structural biology is documented by the fact that over 80% of the more than 80,000 structures in the Protein Data Bank have been determined using synchrotron radiation. X-ray free-electron lasers are expected to extend the capabilities of MX to even more challenging samples. The high brightness of synchrotron sources also allows SAXS measurements at high temporal resolution to characterize overall shapes and dynamics of protein complexes in solution. Synchrotron-radiation circular dichroism (SR-CD) can reveal secondary structures and conformational changes with unprecendented sensitivity. X-ray microscopy analyses thick eukaryotic cells with natural element-specific contrast in their natural hydrated environment, which is a valuable complement to electron tomography.
Synchrotron Infrastructures: DESY (PETRA III, CFEL, X-FEL (from 2015)), HZB (BESSY II), KIT (ANKA)
Users: all participating centres