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; Pedrini, Bill; Frank, Matthias

doi:10.1107/S2052252517017043

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

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.

Authors:

Casadei, Cecilia M.; Tsai, Ching-Ju; Barty, Anton; Hunter, Mark S.;

;

; Capitani, Guido; Benner, W. Henry;

; Hau-Riege, Stefan P.; Kupitz, Christopher;

; Ogren, John I.; Pardini, Tom; Rothschild, Kenneth J.; Sala, Leonardo; Segelke, Brent; Williams, Garth J.; Evans, James E.; Li, Xiao-Dan more »

Publication Date:: Mon Jan 01 00:00:00 EST 2018

Research Org.:: Lawrence Livermore National Lab. (LLNL), Livermore, CA (United States)

Sponsoring Org.:: USDOE National Nuclear Security Administration (NNSA)

OSTI Identifier:: 1437805

Alternate Identifier(s):: OSTI ID: 1557945

Report Number(s):: LLNL-JRNL-782409
Journal ID: ISSN 2052-2525; IUCRAJ; PII: S2052252517017043

Grant/Contract Number:: AC52-07NA27344

Resource Type:: Published Article

Journal Name:: IUCrJ

Additional Journal Information:: Journal Name: IUCrJ Journal Volume: 5 Journal Issue: 1; Journal ID: ISSN 2052-2525

Publisher:: International Union of Crystallography (IUCr)

Country of Publication:: United Kingdom

Language:: English

Subject:: 59 BASIC BIOLOGICAL SCIENCES; serial crystallography; free-electron lasers; membrane proteins; two-dimensional crystals

Citation Formats


                    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, Pedrini, Bill, and Frank, Matthias. Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals.  United Kingdom: N. p., 2018. 
Web.  doi:10.1107/S2052252517017043.

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                    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, Pedrini, Bill, & Frank, Matthias. Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals.  United Kingdom.  https://doi.org/10.1107/S2052252517017043

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                    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, Pedrini, Bill, and Frank, Matthias. Mon .  
"Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals".  United Kingdom.  https://doi.org/10.1107/S2052252517017043.

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@article{osti_1437805,

  title        = {Resolution extension by image summing in serial femtosecond crystallography of two-dimensional membrane-protein crystals},

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

  abstractNote = {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.},

  doi          = {10.1107/S2052252517017043},

  journal      = {IUCrJ},

  number       = 1,

  volume       = 5,

  place        = {United Kingdom},

  year         = {Mon Jan 01 00:00:00 EST 2018},

  month        = {Mon Jan 01 00:00:00 EST 2018}

}

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