A novel two-part method for interpreting X-ray crystallography experiments on protein crystals has been developed by researchers at Cornell University. The method, outlined in a paper published on March 3 in Nature Communications, enables data, which was formerly discarded, to be analysed, leading to a better understanding of a protein’s movement, structure and function. Protein crystallography produces Bragg peaks, which provide high-resolution information about protein structure, as well as capturing cloudy images related to protein movements which are typically ignored. The new method separated these movements and produces a structure of the protein and its atomic movements. The goal is to create a new structural technique – GOODVIBES and DISCOBALL – which researchers can use to test their hypotheses and better scrutinise protein data from X-ray crystallography experiments.
More information: Steve P. Meisburger et al, Robust total X-ray scattering workflow to study correlated motion of proteins in crystals, Nature Communications (2023). DOI: 10.1038/s41467-023-36734-3
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