Industrial Protein X-Ray Crystallography: An Overview

1996 
This presentation provides a change of direction in several respects relative to the other presentations in this symposium. First, rather than dealing with small chemical molecules, I will be considering complex biological macromolecules. Second, whereas the research described in the other presentations has typically been based on limited amounts of data, protein crystal structure determinations require vast amounts of data (from 15,000 to 25,000 independent measurements for a 30 kDa protein structure at 2.0 A resolution). Third, the compounds reported in the other presentations are relatively stable both chemically and with respect to ionizing radiation. But proteins are highly sensitive to both chemical and radiation-induced degradation. And finally, this presentation will describe a general strategy to use synchrotron X-radiation to solve industrially important protein structures, whereas the other presentations have provided detailed case studies of how synchrotron X-ray data have been used to address industrially important problems.
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