Prospects for atomic resolution and neutron crystallography in drug design.
The number of protein crystal structures being refined to atomic resolution is increasing each year as well as the size of proteins being studied. There are currently 346 structures in the protein data bank which have been refined to or beyond atomic resolution. The benefits of atomic resolution X-ray data are discussed along with a number of structural examples of biomedically relevant proteins. The complementary role of neutron diffraction will also be discussed.
Coates
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Division of Biochemistry and Molecular Biology, School of Biological Sciences, University of Southampton, Bassett Crescent East, Southampton SO16 7PX, UK. leighton@soton.ac.uk
Myles
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D000818:Animals; D016880:Anisotropy; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry; D002268:Carboxypeptidases / Q000737:chemistry; D003080:Cold Temperature; D003185:Complement C8 / Q000737:chemistry; D003461:Crystallography; D018360:Crystallography, X-Ray; D015195:Drug Design; D006801:Humans; D033363:Neutron Diffraction; D011506:Proteins / Q000737:chemistry*
D003185:Complement C8; D011506:Proteins; D002268:Carboxypeptidases; D016282:Aspartic Acid Endopeptidases