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Neutron diffraction analysis of the solvent accessible volume in cubic insulin crystals
J Badger1, A Kapulsky, D L Caspar
1Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.
Nature Structural Biology
|January 1, 1995
Abstract:
The average contact distance between protein and solvent surface atoms in cubic insulin crystals has been determined from two sets of 15 A resolution neutron diffraction data. A contact distance between the water hydrogen sites and the protein surface that is significantly shorter than the average protein-water oxygen contact distance implies that many water molecules are oriented with hydrogen atoms pointed towards the protein surface. The shape of the protein/solvent interface is consistent with the protein envelope obtained from atomic co-ordinates.