7 Å resolution in protein twodimensional-crystal X-ray diffraction at Linac Coherent Light Source

Bill Pedrini, Ching Ju Tsai, Guido Capitani, Celestino Padeste, Mark S. Hunter, Nadia Zatsepin, Anton Barty, W. Henry Benner, Sébastien Boutet, Geoffrey K. Feld, Stefan P. Hau-Riege, Richard Kirian, Christopher Kupitz, Marc Messerschmitt, John I. Ogren, Tommaso Pardini, Brent Segelke, Garth J. Williams, John Spence, Rafael Abela & 5 others Matthew Coleman, James E. Evans, Gebhard F X Schertler, Matthias Frank, Xiao Dan Li

    Research output: Contribution to journalArticle

    26 Citations (Scopus)

    Abstract

    Membrane proteins arranged as two-dimensional crystals in the lipid environment provide close-to-physiological structural information, which is essential for understanding the molecular mechanisms of protein function. Previously, X-ray diffraction from individual two-dimensional crystals did not represent a suitable investigational tool because of radiation damage. The recent availability of ultrashort pulses from X-ray free-electron lasers (XFELs) has now provided a means to outrun the damage. Here, we report on measurements performed at the Linac Coherent Light Source XFEL on bacteriorhodopsin two-dimensional crystals mounted on a solid support and kept at room temperature. By merging data from about a dozen single crystal diffraction images, we unambiguously identified the diffraction peaks to a resolution of 7 A, thus improving the observable resolution with respect to that achievable from a single pattern alone. This indicates that a larger dataset will allow for reliable quantification of peak intensities, and in turn a corresponding increase in the resolution. The presented results pave the way for further XFEL studies on two-dimensional crystals, which may include pump-probe experiments at subpicosecond time resolution.

    Original languageEnglish (US)
    Article number20130500
    JournalPhilosophical Transactions of the Royal Society B: Biological Sciences
    Volume369
    Issue number1647
    DOIs
    StatePublished - Jul 17 2014

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    crystal proteins
    X ray lasers
    X-ray diffraction
    X-Ray Diffraction
    crystals
    Light sources
    Free electron lasers
    Lasers
    X-Rays
    Electrons
    crystal
    Light
    X ray diffraction
    Crystals
    protein
    lasers
    X-radiation
    laser
    Bacteriorhodopsins
    electrons

    Keywords

    • Bacteriorhodopsin
    • Crystallographic data analysis
    • Two-dimensional protein crystal
    • X-ray diffraction
    • X-ray free-electron laser

    ASJC Scopus subject areas

    • Agricultural and Biological Sciences(all)
    • Biochemistry, Genetics and Molecular Biology(all)
    • Medicine(all)

    Cite this

    7 Å resolution in protein twodimensional-crystal X-ray diffraction at Linac Coherent Light Source. / Pedrini, Bill; Tsai, Ching Ju; Capitani, Guido; Padeste, Celestino; Hunter, Mark S.; Zatsepin, Nadia; Barty, Anton; Henry Benner, W.; Boutet, Sébastien; Feld, Geoffrey K.; Hau-Riege, Stefan P.; Kirian, Richard; Kupitz, Christopher; Messerschmitt, Marc; Ogren, John I.; Pardini, Tommaso; Segelke, Brent; Williams, Garth J.; Spence, John; Abela, Rafael; Coleman, Matthew; Evans, James E.; Schertler, Gebhard F X; Frank, Matthias; Li, Xiao Dan.

    In: Philosophical Transactions of the Royal Society B: Biological Sciences, Vol. 369, No. 1647, 20130500, 17.07.2014.

    Research output: Contribution to journalArticle

    Pedrini, B, Tsai, CJ, Capitani, G, Padeste, C, Hunter, MS, Zatsepin, N, Barty, A, Henry Benner, W, Boutet, S, Feld, GK, Hau-Riege, SP, Kirian, R, Kupitz, C, Messerschmitt, M, Ogren, JI, Pardini, T, Segelke, B, Williams, GJ, Spence, J, Abela, R, Coleman, M, Evans, JE, Schertler, GFX, Frank, M & Li, XD 2014, '7 Å resolution in protein twodimensional-crystal X-ray diffraction at Linac Coherent Light Source' Philosophical Transactions of the Royal Society B: Biological Sciences, vol. 369, no. 1647, 20130500. https://doi.org/10.1098/rstb.2013.0500
    Pedrini, Bill ; Tsai, Ching Ju ; Capitani, Guido ; Padeste, Celestino ; Hunter, Mark S. ; Zatsepin, Nadia ; Barty, Anton ; Henry Benner, W. ; Boutet, Sébastien ; Feld, Geoffrey K. ; Hau-Riege, Stefan P. ; Kirian, Richard ; Kupitz, Christopher ; Messerschmitt, Marc ; Ogren, John I. ; Pardini, Tommaso ; Segelke, Brent ; Williams, Garth J. ; Spence, John ; Abela, Rafael ; Coleman, Matthew ; Evans, James E. ; Schertler, Gebhard F X ; Frank, Matthias ; Li, Xiao Dan. / 7 Å resolution in protein twodimensional-crystal X-ray diffraction at Linac Coherent Light Source. In: Philosophical Transactions of the Royal Society B: Biological Sciences. 2014 ; Vol. 369, No. 1647.
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    AU - Pedrini, Bill

    AU - Tsai, Ching Ju

    AU - Capitani, Guido

    AU - Padeste, Celestino

    AU - Hunter, Mark S.

    AU - Zatsepin, Nadia

    AU - Barty, Anton

    AU - Henry Benner, W.

    AU - Boutet, Sébastien

    AU - Feld, Geoffrey K.

    AU - Hau-Riege, Stefan P.

    AU - Kirian, Richard

    AU - Kupitz, Christopher

    AU - Messerschmitt, Marc

    AU - Ogren, John I.

    AU - Pardini, Tommaso

    AU - Segelke, Brent

    AU - Williams, Garth J.

    AU - Spence, John

    AU - Abela, Rafael

    AU - Coleman, Matthew

    AU - Evans, James E.

    AU - Schertler, Gebhard F X

    AU - Frank, Matthias

    AU - Li, Xiao Dan

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    N2 - Membrane proteins arranged as two-dimensional crystals in the lipid environment provide close-to-physiological structural information, which is essential for understanding the molecular mechanisms of protein function. Previously, X-ray diffraction from individual two-dimensional crystals did not represent a suitable investigational tool because of radiation damage. The recent availability of ultrashort pulses from X-ray free-electron lasers (XFELs) has now provided a means to outrun the damage. Here, we report on measurements performed at the Linac Coherent Light Source XFEL on bacteriorhodopsin two-dimensional crystals mounted on a solid support and kept at room temperature. By merging data from about a dozen single crystal diffraction images, we unambiguously identified the diffraction peaks to a resolution of 7 A, thus improving the observable resolution with respect to that achievable from a single pattern alone. This indicates that a larger dataset will allow for reliable quantification of peak intensities, and in turn a corresponding increase in the resolution. The presented results pave the way for further XFEL studies on two-dimensional crystals, which may include pump-probe experiments at subpicosecond time resolution.

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