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J Biol Chem, Vol. 274, Issue 30, 20753-20755, July 23, 1999

COMMUNICATION
Experimental Observation of Bonding Electrons in Proteins

Victor S. LamzinDagger , Richard J. MorrisDagger , Zbigniew Dauter, Keith S. WilsonDagger parallel , and Martha M. Teeter**

From the Dagger  European Molecular Biology Laboratory, 22603 Hamburg, Germany, the  National Cancer Institute, Upton, New York 11973, the parallel  University of York, Heslington, York, Y01 5DD, United Kingdom, and the ** Department of Chemistry, Merkert Chemistry, Boston College, Chestnut Hill, Massachusetts 02167

We demonstrate with two examples the success and potential of recent developments in x-ray protein crystallography at ultra high resolution. Our preliminary structural analyses using diffraction data collected for the two proteins crambin and savinase show meaningful deviations from the conventional independent spherical atom approximation. A noise-reduction averaging technique enables bonding details of electron distributions in proteins to be revealed experimentally for the first time. We move one step closer to imaging directly the fine details of the electronic structure on which the biological function of a protein is based.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.