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The impact of synchrotron radiation in protein crystallography

A full understanding of biological processes requires the knowledge of the structure of the biomolecules involved, along with their interactions with other molecules. These structures can also lead to the design of improved therapeutic agents for pathologies that involve these proteins. Recently the sequencing of the genomes of numerous organisms has accelerated the need for performing structural studies on the gene products as an approach to understanding their function. In these regards, the use of X-ray crystallography with synchrotron radiation (SR) has proven itself to be a necessity. The properties of SR that make it so valuable are the flux and brightness of the X-ray beams produced, along with the ability to tune the energy to the absorption edge of elements in the crystal such as selenium, mercury, iridium, etc., in order to measure the data for producing tlie phases necessary for calculating an electron density map. These properties allow for the collection-of data from microcrystals, and from crystals with large unit cell dimensions, as well as extremely rapid structure determination. Perhaps more than any other field, biological crystallography has benefited from the use of X-rays produced by synchrotrons.