Non-thermal microwave effects on protein dynamics? An X-ray diffraction study on tetragonal lysozyme crystals

X-ray diffraction (XRD) was used to investigate the structural and dynamical effects of microwave fields on tetragonal single crystals of hen egg-white lysozyme at a resolution of 2.0 A. Using a modified slab-line waveguide allows on-line XRD to be carried out while the protein crystal is exposed to well defined microwave fields. High microwave power levels mainly lead to increased, but largely recoverable, lattice defects owing to the evaporation of crystal water. At lower microwave power levels, the presence of the microwave field results in localized reproducible changes in the mean-square displacements (B factors). At particular sites, it is found that the B factors even decrease with increasing microwave power. Most of these effects can be explained by a comparison of the data obtained under microwave irradiation with data obtained at elevated temperature which simulate heating owing to microwave absorption by unbound crystal water. The data show no indication of large microwave-driven displacements of structural subunits in the protein that would be expected if microwaves were to be absorbed resonantly by protein vibrations. Rather, the observed changes in the atomic mean-square displacements suggest that if microwaves couple non-thermally to globular proteins at hydration levels at which they still function, their effect on protein dynamics and structure is very small.