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This lecture covers the methods used for protein structure determination, focusing on X-ray crystallography and Nuclear Magnetic Resonance (NMR) spectroscopy. It delves into the historical significance of structural biology, the process of obtaining protein crystals, crystallization screening conditions, and the interpretation of diffraction patterns. The lecture also explains the principles of Bragg's Law of Diffraction, the transition from crystal to structure refinement, and the challenges of protein crystallization. Additionally, it explores the use of NMR in protein structure determination, isotope labeling, and the contributions of Kurt Wüthrich to biomolecular NMR spectroscopy.