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Application of In Situ Diffraction in High-Throughput Structure Determination Platforms

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Structural Proteomics

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1261))

Abstract

Macromolecular crystallography (MX) is the most powerful technique available to structural biologists to visualize in atomic detail the macromolecular machinery of the cell. Since the emergence of structural genomics initiatives, significant advances have been made in all key steps of the structure determination process. In particular, third-generation synchrotron sources and the application of highly automated approaches to data acquisition and analysis at these facilities have been the major factors in the rate of increase of macromolecular structures determined annually. A plethora of tools are now available to users of synchrotron beamlines to enable rapid and efficient evaluation of samples, collection of the best data, and in favorable cases structure solution in near real time. Here, we provide a short overview of the emerging use of collecting X-ray diffraction data directly from the crystallization experiment. These in situ experiments are now routinely available to users at a number of synchrotron MX beamlines. A practical guide to the use of the method on the MX suite of beamlines at Diamond Light Source is given.

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Author information

Authors and Affiliations

  1. Diamond Light Source Ltd., Diamond House, Harwell Science and Innovation Campus, Chilton, Didcot, Oxfordshire, OX11 0DE, UK

    Pierre Aller, Juan Sanchez-Weatherby, James Foadi, Graeme Winter, Carina M. C. Lobley, Danny Axford, Alun W. Ashton, Domenico Bellini, Jose Brandao-Neto, Simone Culurgioni, Alice Douangamath, Ramona Duman, Gwyndaf Evans, Stuart Fisher, Ralf Flaig, David R. Hall, Petra Lukacik, Marco Mazzorana, Katherine E. McAuley, Vitaliy Mykhaylyk, Robin L. Owen, Neil G. Paterson, Pierpaolo Romano, James Sandy, Thomas Sorensen, Frank von Delft, Armin Wagner, Anna Warren, Mark Williams, David I. Stuart & Martin A. Walsh

  2. Division of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford, OX3 7BN, UK

    David I. Stuart

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  1. Pierre Aller
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  2. Juan Sanchez-Weatherby
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  13. Gwyndaf Evans
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  27. Armin Wagner
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  28. Anna Warren
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  29. Mark Williams
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  31. Martin A. Walsh
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Corresponding author

Correspondence to Martin A. Walsh .

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Editors and Affiliations

  1. Oxford Protein Production Facility UK, Didcot, Oxfordshire, United Kingdom

    Raymond J. Owens

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Aller, P. et al. (2015). Application of In Situ Diffraction in High-Throughput Structure Determination Platforms. In: Owens, R. (eds) Structural Proteomics. Methods in Molecular Biology, vol 1261. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2230-7_13

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  • DOI: https://doi.org/10.1007/978-1-4939-2230-7_13

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  • Publisher Name: Humana Press, New York, NY

  • Print ISBN: 978-1-4939-2229-1

  • Online ISBN: 978-1-4939-2230-7

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