Molecular Dynamics (MD) and Monte Carlo (MC) simulations of crystals can help in interpretation of experimental X-ray crystallography data. Particularly, they can be useful for understanding how various crystallization techniques affect protein conformational plasticity within the crystal lattice and the stability of biomolecular crystals. The latter has become especially important since the modern and extremely intense X-ray radiation sources (such as free electron lasers, FELs) appeared recently.
In the present study we were able to show by means of computer simulations that the lysozyme crystals obtained using the Langmuir-Blodgett technique have an advantage over the classical ones (“Hanging Drop”) in terms of their thermal stability as well as their stability against the radiation damage. We also demonstrate an important role of crystal water dynamics for stability of protein crystals.

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