Most structures are determined by X-ray diffraction, but about 7% of structures are determined by protein NMR. When using X-ray diffraction, approximations of the coordinates of the atoms of the protein are obtained, whereas using NMR, the distance between pairs of atoms of the protein is estimated. The final conformation of the protein is obtained from NMR by solving a distance geometry problem. After 2013, a growing number of proteins are determined by cryo-electron microscopy.
Most structures are determined by X-ray diffraction, but about 7% of structures are determined by protein NMR When using X-ray diffraction, approximations of the coordinates of the atoms of the protein are obtained, whereas using NMR the distance between pairs of atoms of the protein is estimated The final conformation of the protein is obtained from NMR by solving a distance geometry problem. After 2013, a growing number of proteins are determined by cryo-electron microscopy.