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Studying Protein–Ligand Interactions Using X-Ray Crystallography

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Protein-Ligand Interactions

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1008))

Abstract

X-ray crystallography is a powerful technique for studying protein–ligand interactions. Advances in techniques have meant that it is now possible to routinely determine the structures of ligand complexes in the majority of cases where crystallization conditions and protein structures are already known. Ligand soaking or cocrystallization, together with the potential use of molecular replacement, provides data for determining the structures of a protein in complex with ligands. Furthermore, advances in protein structure model building facilitate automatic ligand fitting to residual electron density in the protein–ligand complex.

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Author information

Authors and Affiliations

  1. CRT Discovery Laboratories, Department of Biological Sciences, Birkbeck, University of London, London, UK

    Andrew P. Turnbull

  2. Structural Studies, MRC Laboratory of Molecular Biology, Cambridge, UK

    Paul Emsley

Authors
  1. Andrew P. Turnbull
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  2. Paul Emsley
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Editor information

Editors and Affiliations

  1. Birbeck, University of London, ISMB Biophysics Centre, Institute of Str, Malet Street, London, WC1E 7HX, United Kingdom

    Mark A. Williams

  2. Birkbeck, University of London, School of Crystallography, ISMB Biophysics Centre, Institute of Str, Malet Street, London, WC1E 7HX, United Kingdom

    Tina Daviter

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Turnbull, A.P., Emsley, P. (2013). Studying Protein–Ligand Interactions Using X-Ray Crystallography. In: Williams, M., Daviter, T. (eds) Protein-Ligand Interactions. Methods in Molecular Biology, vol 1008. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-398-5_17

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  • DOI: https://doi.org/10.1007/978-1-62703-398-5_17

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-62703-397-8

  • Online ISBN: 978-1-62703-398-5

  • eBook Packages: Springer Protocols

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