single-wavelength anomalous diffraction (sad) is a technique used in x-ray crystallography that facilitates the determination of the structure of proteins or other biological macromolecules by allowing the solution of the phase problem. in contrast to multi-wavelength anomalous diffraction, sad uses a single dataset at a single appropriate wavelength. one advantage of the technique is the minimization of time spent in the beam by the crystal, thus reducing potential radiation damage to the molecule while collecting data. sad is sometimes called "single-wavelength anomalous dispersion", but no dispersive differences are used in this technique since the data are collected at a single wavelength.