Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals

Cecilia M. Casadei; Ching Ju Tsai; Anton Barty; Mark S. Hunter; Nadia A. Zatsepin; Celestino Padeste; Guido Capitani; W. Henry Benner; Sébastien Boutet; Stefan P. Hau-Riege; Christopher Kupitz; Marc Messerschmidt; John I. Ogren; Tom Pardini; Kenneth J. Rothschild; Leonardo Sala; Brent Segelke; Garth J. Williams; James E. Evans; Xiao Dan Li; Matthew A Coleman; Bill Pedrini; Matthias Frank

doi:10.1107/S2052252517017043

Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals

Cecilia M. Casadei, Ching Ju Tsai, Anton Barty, Mark S. Hunter, Nadia A. Zatsepin, Celestino Padeste, Guido Capitani, W. Henry Benner, Sébastien Boutet, Stefan P. Hau-Riege, Christopher Kupitz, Marc Messerschmidt, John I. Ogren, Tom Pardini, Kenneth J. Rothschild, Leonardo Sala, Brent Segelke, Garth J. Williams, James E. Evans, Xiao Dan LiMatthew A Coleman, Bill Pedrini, Matthias Frank

Research output: Contribution to journal › Article

7 Scopus citations

Abstract

Previous proof-of-concept measurements on single-layer two-dimensional membrane-protein crystals performed at X-ray free-electron lasers (FELs) have demonstrated that the collection of meaningful diffraction patterns, which is not possible at synchrotrons because of radiation-damage issues, is feasible. Here, the results obtained from the analysis of a thousand single-shot, room-temperature X-ray FEL diffraction images from two-dimensional crystals of a bacteriorhodopsin mutant are reported in detail. The high redundancy in the measurements boosts the intensity signal-to-noise ratio, so that the values of the diffracted intensities can be reliably determined down to the detector-edge resolution of 4'Å. The results show that two-dimensional serial crystallography at X-ray FELs is a suitable method to study membrane proteins to near-atomic length scales at ambient temperature. The method presented here can be extended to pump-probe studies of optically triggered structural changes on submillisecond timescales in two-dimensional crystals, which allow functionally relevant large-scale motions that may be quenched in three-dimensional crystals.

Original language	English (US)
Pages (from-to)	103-117
Number of pages	15
Journal	IUCrJ
Volume	5
DOIs	https://doi.org/10.1107/S2052252517017043
State	Published - Jan 1 2018
Externally published	Yes

Keywords

free-electron lasers
membrane proteins
serial crystallography
two-dimensional crystals

ASJC Scopus subject areas

Chemistry(all)
Biochemistry
Materials Science(all)
Condensed Matter Physics

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Casadei, C. M., Tsai, C. J., Barty, A., Hunter, M. S., Zatsepin, N. A., Padeste, C., Capitani, G., Benner, W. H., Boutet, S., Hau-Riege, S. P., Kupitz, C., Messerschmidt, M., Ogren, J. I., Pardini, T., Rothschild, K. J., Sala, L., Segelke, B., Williams, G. J., Evans, J. E., ... Frank, M. (2018). Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals. IUCrJ, 5, 103-117. https://doi.org/10.1107/S2052252517017043

Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals. / Casadei, Cecilia M.; Tsai, Ching Ju; Barty, Anton; Hunter, Mark S.; Zatsepin, Nadia A.; Padeste, Celestino; Capitani, Guido; Benner, W. Henry; Boutet, Sébastien; Hau-Riege, Stefan P.; Kupitz, Christopher; Messerschmidt, Marc; Ogren, John I.; Pardini, Tom; Rothschild, Kenneth J.; Sala, Leonardo; Segelke, Brent; Williams, Garth J.; Evans, James E.; Li, Xiao Dan; Coleman, Matthew A; Pedrini, Bill; Frank, Matthias.

In: IUCrJ, Vol. 5, 01.01.2018, p. 103-117.

Research output: Contribution to journal › Article

Casadei, CM, Tsai, CJ, Barty, A, Hunter, MS, Zatsepin, NA, Padeste, C, Capitani, G, Benner, WH, Boutet, S, Hau-Riege, SP, Kupitz, C, Messerschmidt, M, Ogren, JI, Pardini, T, Rothschild, KJ, Sala, L, Segelke, B, Williams, GJ, Evans, JE, Li, XD, Coleman, MA, Pedrini, B & Frank, M 2018, 'Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals', IUCrJ, vol. 5, pp. 103-117. https://doi.org/10.1107/S2052252517017043

Casadei, Cecilia M. ; Tsai, Ching Ju ; Barty, Anton ; Hunter, Mark S. ; Zatsepin, Nadia A. ; Padeste, Celestino ; Capitani, Guido ; Benner, W. Henry ; Boutet, Sébastien ; Hau-Riege, Stefan P. ; Kupitz, Christopher ; Messerschmidt, Marc ; Ogren, John I. ; Pardini, Tom ; Rothschild, Kenneth J. ; Sala, Leonardo ; Segelke, Brent ; Williams, Garth J. ; Evans, James E. ; Li, Xiao Dan ; Coleman, Matthew A ; Pedrini, Bill ; Frank, Matthias. / Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals. In: IUCrJ. 2018 ; Vol. 5. pp. 103-117.

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abstract = "Previous proof-of-concept measurements on single-layer two-dimensional membrane-protein crystals performed at X-ray free-electron lasers (FELs) have demonstrated that the collection of meaningful diffraction patterns, which is not possible at synchrotrons because of radiation-damage issues, is feasible. Here, the results obtained from the analysis of a thousand single-shot, room-temperature X-ray FEL diffraction images from two-dimensional crystals of a bacteriorhodopsin mutant are reported in detail. The high redundancy in the measurements boosts the intensity signal-to-noise ratio, so that the values of the diffracted intensities can be reliably determined down to the detector-edge resolution of 4'{\AA}. The results show that two-dimensional serial crystallography at X-ray FELs is a suitable method to study membrane proteins to near-atomic length scales at ambient temperature. The method presented here can be extended to pump-probe studies of optically triggered structural changes on submillisecond timescales in two-dimensional crystals, which allow functionally relevant large-scale motions that may be quenched in three-dimensional crystals.",

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AU - Casadei, Cecilia M.

AU - Tsai, Ching Ju

AU - Barty, Anton

AU - Hunter, Mark S.

AU - Zatsepin, Nadia A.

AU - Padeste, Celestino

AU - Capitani, Guido

AU - Benner, W. Henry

AU - Boutet, Sébastien

AU - Hau-Riege, Stefan P.

AU - Kupitz, Christopher

AU - Messerschmidt, Marc

AU - Ogren, John I.

AU - Pardini, Tom

AU - Rothschild, Kenneth J.

AU - Sala, Leonardo

AU - Segelke, Brent

AU - Williams, Garth J.

AU - Evans, James E.

AU - Li, Xiao Dan

AU - Coleman, Matthew A

AU - Pedrini, Bill

AU - Frank, Matthias

PY - 2018/1/1

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N2 - Previous proof-of-concept measurements on single-layer two-dimensional membrane-protein crystals performed at X-ray free-electron lasers (FELs) have demonstrated that the collection of meaningful diffraction patterns, which is not possible at synchrotrons because of radiation-damage issues, is feasible. Here, the results obtained from the analysis of a thousand single-shot, room-temperature X-ray FEL diffraction images from two-dimensional crystals of a bacteriorhodopsin mutant are reported in detail. The high redundancy in the measurements boosts the intensity signal-to-noise ratio, so that the values of the diffracted intensities can be reliably determined down to the detector-edge resolution of 4'Å. The results show that two-dimensional serial crystallography at X-ray FELs is a suitable method to study membrane proteins to near-atomic length scales at ambient temperature. The method presented here can be extended to pump-probe studies of optically triggered structural changes on submillisecond timescales in two-dimensional crystals, which allow functionally relevant large-scale motions that may be quenched in three-dimensional crystals.

AB - Previous proof-of-concept measurements on single-layer two-dimensional membrane-protein crystals performed at X-ray free-electron lasers (FELs) have demonstrated that the collection of meaningful diffraction patterns, which is not possible at synchrotrons because of radiation-damage issues, is feasible. Here, the results obtained from the analysis of a thousand single-shot, room-temperature X-ray FEL diffraction images from two-dimensional crystals of a bacteriorhodopsin mutant are reported in detail. The high redundancy in the measurements boosts the intensity signal-to-noise ratio, so that the values of the diffracted intensities can be reliably determined down to the detector-edge resolution of 4'Å. The results show that two-dimensional serial crystallography at X-ray FELs is a suitable method to study membrane proteins to near-atomic length scales at ambient temperature. The method presented here can be extended to pump-probe studies of optically triggered structural changes on submillisecond timescales in two-dimensional crystals, which allow functionally relevant large-scale motions that may be quenched in three-dimensional crystals.

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