Radial distributions of water—water distances in protein crystals

Abstract

An accurate protein crystallographic structure determination requires a knowledge of the solvent contribution to the diffraction pattern. As resolutions improve, research groups are reporting coordinates of large numbers of water molecules. We examine the accuracy of these coordinates by presenting radial distributions of water—water distances from refinements at different stages and interpreting them in terms of preferred hydrogen-bonding distances and problems in solvent electron density map interpretation. Marked differences between the distributions suggest that wide variations exist in the water molecule selection and refinement criteria employed by different research groups which mask possible real differences in solvent structure.