Experimental observation of bonding electrons in proteins

被引:19
作者
Lamzin, VS [1 ]
Morris, RJ
Dauter, Z
Wilson, KS
Teeter, MM
机构
[1] European Mol Biol Lab, D-22603 Hamburg, Germany
[2] NCI, Upton, NY 11973 USA
[3] Univ York, York YO1 5DD, N Yorkshire, England
[4] Boston Coll, Dept Chem, Chestnut Hill, MA 02167 USA
关键词
D O I
10.1074/jbc.274.30.20753
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:20753 / 20755
页数:3
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