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Combined Use of XAFS and Crystallography for Studying Protein-Ligand Interactions in Metalloproteins

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Protein-Ligand Interactions

Part of the book series: Methods in Molecular Biology ((MIMB,volume 305))

Abstract

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 ligandbinding 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 threedimensional 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.

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Author information

Authors and Affiliations

  1. Molecular Biophysics Group, College of Biology and Medicine, CCLRC Daresbury Laboratory, Daresbury, Warrington, Cheshire, UK

    Richard W. Strange & S. Samar Hasnain

Authors
  1. Richard W. Strange
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  2. S. Samar Hasnain
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Editors and Affiliations

  1. Department of Biophysics, University of Ulm, Ulm, Germany

    G. Ulrich Nienhaus

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© 2005 Humana Press Inc., Totowa, NJ

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Strange, R.W., Hasnain, S.S. (2005). Combined Use of XAFS and Crystallography for Studying Protein-Ligand Interactions in Metalloproteins. In: Ulrich Nienhaus, G. (eds) Protein-Ligand Interactions. Methods in Molecular Biology, vol 305. Humana, Totowa, NJ. https://doi.org/10.1385/1-59259-912-5:167

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  • DOI: https://doi.org/10.1385/1-59259-912-5:167

  • Publisher Name: Humana, Totowa, NJ

  • Print ISBN: 978-1-58829-372-5

  • Online ISBN: 978-1-59259-912-7

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