Computer simulation of the dynamics of hydrated protein crystals and its comparison with x-ray data

The structure and dynamics of the full unit cell of a protein (bovine pancreatic trypsin inhibitor) containing 4 protein molecules and 560 water molecules have been simulated by using the molecular dynamics method. The obtained structure, atom positional fluctuations, and structure factors are compared with x-ray values. A way of calculating the motional contributions to structure factors is proposed.