How x-ray diffraction with synchrotron radiation got started
Synchrotron radiation has proved to be of inestimable importance for extending the scope of x-ray diffraction methodology for protein crystallography. The laser-like optics and tremendous brilliance allow x-ray diffraction data to be collected from ever smaller crystals of ever larger complexes and organelles. In addition, the ability to select wavelengths makes it possible to exploit anomalous scattering for phase determination (MAD). Moreover, the continuous spectrum makes it possible, in favourable cases, to obtain data in fractions of a second. Within the next decade genome sequencing projects will provide us with a complete menu of all DNA, RNA, and protein molecules in a number of organisms and will thereby give us the inventory of life. To make full use of all these data we will need to understand the macromolecular interactions which control cell signalling, cell locomotion and gene activation. To do this we will need a detailed description of the structure of many of the relevant macromolecules. At present, only x-ray protein crystallography yields a molecular anatomy of adequate resolution and precision for this task. Thus there would seem to be an almost limitless need for x-ray crystallography groups working on proteins if full use is to be made of the flood of genetic information arising from the sequencing projects.
However, this is not how x-ray diffraction with synchrotron light got started, it started with muscle.