Water structure in vitamin B12 coenzyme crystals. II. Structural characteristics of the solvent networks.

The geometrical details of the solvent structure in vitamin B12 coenzyme crystals with respect to hydrogen bonding and nonbonded contacts, are described. The individual H-bond geometries varied over wide ranges, similar to those observed in small molecule structures. Large deviations from tetrahedral coordination were found around a majority of the waters. The mutual positions and orientations of the water molecules could not be adequately explained in terms of the H-bonding relationships present in the structure. However, additional investigations, which focused on the short range nonbonded contacts around water positions in a variety of crystal hydrates, revealed several structural regularities (Savage, 1986b). These features relate to the nonbonded O...O, H...O, and H...H interactions, and give rise to a set of repulsive restrictions that are seen to be very much stronger stereochemical restraints than those associated with H-bonding. The short-range restrictions appear largely to govern the local orientational correlations and packing arrangements of the water structure within the coenzyme (and other hydrate) crystals. In more general terms, the inclusion of the nonbonding relationships as well as the attractive H-bonding interactions, leads to a significant increase in our understanding of water structure(s). The repulsive restrictions can be used as stereochemical restraints in the interpretation and refinement of solvent structures within larger hydrate systems, such as protein crystals. They may also be included in potential functions used to simulate solvent structures in aqueous solutions and hydrate systems.