Repulsive restraints for hydrogen bonding in least-squares refinement of protein crystals. A neutron diffraction study of myoglobin crystals

The purpose of this article is to describe stereochemical restraints on hydrogen bonding within proteins and their associated solvent which can be included in the refinement (PROLSQ) of X-ray or neutron structures of protein crystals. The parameters which define the geometry of hydrogen bonding, i.e. the correlation between distances and angles, are based on the results of an analysis of hydrogen bonding in crystal structures of myoglobin derivatives analyzed by neutron diffraction. (orig.)