THE USE OF SYNCHROTRON-RADIATION IN PROTEIN CRYSTALLOGRAPHY

Synchrotron radiation provides a source of high intensity, wavelength tunable, highly collimated radiation which can be used to investigate structure-function relationships in biological macromolecules in a number of ways. This chapter will deal mainly with the applications of the hard X-ray region (0.5-2.5 Angstrom) of the synchrotron spectrum to 3-D structure analysis of single crystals of macromolecules. The main themes highlighted will be; (a) why synchrotron radiation is necessary for structural studies on biological macromolecules, (b) examples of experimental stations used for protein crystallography at the Synchrotron Radiation Source, SERC Daresbury Laboratory, (c) how the wavelength tunability can be exploited to solve the ''phase problem'', (d) structural studies with the ''white beam'', (e) high resolution data using cryogenic methods and (f) studies on large structures.