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

27 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 - Tsai, Ching Ju

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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.

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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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