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

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Keywords

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

ASJC Scopus subject areas

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

Cite this

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 - Zatsepin, Nadia A.

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10.1107/S2052252517017043