Volbeda Anne
Metalloproteins Unit, Institut de Biologie Structurale, UMR 5075 CEA-CNRS-UJF, 6 rue Jules Horowitz, 38000, Grenoble, France,
Methods Mol Biol. 2014;1122:189-206. doi: 10.1007/978-1-62703-794-5_13.
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.
许多蛋白质需要金属来发挥其生理功能。结合光谱表征，X射线晶体学是一种非常强大的方法，可将蛋白质结合金属位点的功能与其结构相关联。由于特定金属具有特殊的X射线散射特性，它们可定位在金属蛋白结构中，并最终通过多波长反常色散（MAD）方法用于对衍射X射线进行相位测定。本章的主要主题就是介绍其具体操作方法。同时还会关注氧化还原活性金属不同氧化态的晶体学表征，以及蛋白质晶体的X射线照射可能引起的结构变化的复杂性。
