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A method has been developed to determine the structure of bound solvent and the positions of exchanged hydrogens in proteins, on the basis of neutron diffraction from hydrogenous and deuterated crystals. In this method phases for the hydrogenous and for the deuterated model are refined simultaneously, and an average model is imposed in the volume occupied by non-hydrogen atoms. The densities in the areas of bulk solvent are replaced by their average values, while no modifications are performed in the vicinity of ordered solvents and potentially exchangeable hydrogens. The method was tested on 1.8 Å neutron diffraction data collected from two crystals of bovine pancreatic trypsin inhibitor, one of them deuterated and the other hydrogenous. Significant improvement was observed for the densities corresponding to many partially occupied solvent sites, as well as to partially exchanged hydrogens. The algorithm presented here has been compared with a different approach published recently by Shpungin & Kossiakoff [Methods Enzymol. (1986), 127, 329-342].
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