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.
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Acknowledgements
This work was supported by institutional funding from the Commissariat à l’Energie Atomique et aux Energies Alternatives (CEA) and the Centre National de la Recherche Scientifique (CNRS). The author wishes to thank David Cobessi and Jean-Luc Ferrer of the Synchrotron Group of the IBS for helpful discussions.
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Volbeda, A. (2014). X-Ray Crystallographic Studies of Metalloproteins. In: Fontecilla-Camps, J., Nicolet, Y. (eds) Metalloproteins. Methods in Molecular Biology, vol 1122. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-794-5_13
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