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Proteins are small (molecular) machines which are involved in all kinds of cellular processes in living organisms. Their function is determined by their three-dimensional molecular structure, which can be studied with a technique called X-ray crystallography.

The structure on its own does not tell the full story, because proteins are highly dynamic and flexible molecules. For this project, we developed a new method which can provide a molecular picture of protein motions in a crystal as derived from diffuse scattering data. We combine simulations on small crystalline models with diffuse scattering data from X-ray diffraction experiments.

We found that in a crystal, the largest motion component in the experimental data is that of the entire protein molecule, and that the motions of smaller (internal) parts of the protein are present but less pronounced.