How does X-Ray Crystallography separate proteins?
Answer: Highly ordered crystalline specimens are exposed to an X-ray beam. As the rays hit the crystal, they are scattered by atoms in the crystal. The diffraction patterns are used to construct an electron density map, as the resolving power of X-ray crystallography is equivalent to interatomic distances. A computer is then used to reconstruct a 3D model of the polypeptide using the electron density map.