Abstract
Most of the current knowledge concerning the water structure in and around biological macromolecules has been derived at near-atomic resolution from high-resolution X-ray and neutron diffraction studies of crystals (for review, see Finney, 1979; Edsall and McKenzie, 1983; Baker and Hubbard; 1984; Savage and Wlodawer, 1986; Saenger, 1987; Westhof, 1988; Westhof and Beveridge, 1990; Rupley and Caveri, 1991). Protein crystals, like nucleic acid crystals, are made up of a lattice of macromolecules which delimit channels of variable dimensions filled with solvent molecules. They constitute, thus, a suitable system to study the interactions between protein and water molecules at the atomic level, under conditions which are, to some extent, close to those found in solution.
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