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The DUX4 protein is a key player for the development of FSHD and constitutes a primary target for drug therapy. In order to understand the function of DUX4 and devise molecular models for drugs that inhibit its function, it is essential to know the three-dimensional structure of DUX4 at the atomic level. In this research proposal, we will use a combined approach including X-ray crystallography and NMR spectroscopy to determine the structure of DUX4 DNA-binding domain free and bound to its target DNA. This synergistic approach will make it possible to determine the motions of the protein both free and in the bound state and identify sites for rational drug design.