title: X-ray crystallographic studies of metalloproteins.
abstract: Many proteins require metals for their physiological function. In combination with spectroscopic characterizations, X-ray crystallography is a very powerful method to correlate the function of protein-bound metal sites with their structure. Due to their special X-ray scattering properties, specific metals may be located in metalloprotein structures and eventually used for phasing the diffracted X-rays by the method of Multi-wavelength Anomalous Dispersion (MAD). How this is done is the principle subject of this chapter. Attention is also given to the crystallographic characterization of different oxidation states of redox active metals and to the complication of structural changes that may be induced by X-ray irradiation of protein crystals.
authors.affiliation: Metalloproteins Unit, Institut de Biologie Structurale, UMR 5075 CEA-CNRS-UJF, 6 rue Jules Horowitz, 38000, Grenoble, France, anne.volbeda@ibs.fr.
authors.forename: Anne
authors.initials: A
authors.lastname: Volbeda
mesh_terms: D065966:Absorption, Physicochemical; D001426:Bacterial Proteins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D004602:Elements; D008667:Metalloproteins / Q000737:chemistry*; D008958:Models, Molecular; D058845:Moorella / Q000378:metabolism; D010084:Oxidation-Reduction; D012542:Scattering, Radiation; D013050:Spectrometry, Fluorescence; D056928:X-Ray Absorption Spectroscopy
chemical_list: D001426:Bacterial Proteins; D004602:Elements; D008667:Metalloproteins