Combined use of XAFS and crystallography for studying protein-ligand interactions in metalloproteins.

This chapter describes the method of X-ray absorption spectroscopy when applied to the study of metal sites in proteins. The method requires the intense X-rays found only at synchrotron radiation sources, and is equally applicable to metalloproteins in dilute solutions, in fibers, films, and in crystalline states. In each case, structural changes occurring at metal sites during catalysis or ligand-binding are revealed with an accuracy and precision equivalent to atomic resolution crystallography. When combined with crystallographic data, of any resolution, X-ray absorption spectroscopy can yield atomic resolution three-dimensional structural models of the metal sites, thus providing the level of structural detail necessary for understanding the chemical mechanisms involved in the active states of metalloproteins.