What is an advantage of X-ray crystallography over nuclear magnetic resonance spectroscopy for protein structure determination?

One important advantage of X-ray crystallography over NMR spectroscopy for protein structure determination is its ability to provide higher resolution details of protein structures. This allows for more accurate and detailed analysis of the three-dimensional structure of proteins, including their atomic positions, the arrangement of amino acid residues, and any interactions between them. X-ray crystallography works by directing an intense X-ray beam at a crystallized sample of the protein, which then scatters the X-rays in various directions. The resulting diffraction patterns are analyzed to determine the electron density of the protein, which in turn reveals the protein's three-dimensional structure at atomic resolution. NMR spectroscopy, on the other hand, relies on the magnetic properties of atomic nuclei, specifically their response to an applied magnetic field. While NMR can provide information about the distances between atoms and the local environment of certain nuclei, the resolution of the resulting data tends to be lower than that obtained with X-ray crystallography, especially for larger proteins. In summary, an advantage of X-ray crystallography over NMR spectroscopy for protein structure determination is its ability to provide higher resolution details of protein structures, allowing for more accurate analyses of their three-dimensional arrangements and interactions.