skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals

Abstract

Serial femtosecond crystallography of two-dimensional membrane-protein crystals at X-ray free-electron lasers has the potential to address the dynamics of functionally relevant large-scale motions, which can be sterically hindered in three-dimensional crystals and suppressed in cryocooled samples. In previous work, diffraction data limited to a two-dimensional reciprocal-space slice were evaluated and it was demonstrated that the low intensity of the diffraction signal can be overcome by collecting highly redundant data, thus enhancing the achievable resolution. Here, the application of a newly developed method to analyze diffraction data covering three reciprocal-space dimensions, extracting the reciprocal-space map of the structure-factor amplitudes, is presented. Despite the low resolution and completeness of the data set, it is shown by molecular replacement that the reconstructed amplitudes carry meaningful structural information. Therefore, it appears that these intrinsic limitations in resolution and completeness from two-dimensional crystal diffraction may be overcome by collecting highly redundant data along the three reciprocal-space axes, thus allowing the measurement of large-scale dynamics in pump–probe experiments.

Authors:
; ORCiD logo; ; ; ORCiD logo; ; ORCiD logo; ; ; ; ; ; ; ;
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1481810
Grant/Contract Number:  
AC52-07NA27344; AC02-76SF00515; SC0012704
Resource Type:
Journal Article: Published Article
Journal Name:
IUCrJ
Additional Journal Information:
Journal Name: IUCrJ Journal Volume: 6 Journal Issue: 1; Journal ID: ISSN 2052-2525
Publisher:
International Union of Crystallography (IUCr)
Country of Publication:
United Kingdom
Language:
English

Citation Formats

Casadei, Cecilia M., Nass, Karol, Barty, Anton, Hunter, Mark S., Padeste, Celestino, Tsai, Ching-Ju, Boutet, Sébastien, Messerschmidt, Marc, Sala, Leonardo, Williams, Garth J., Ozerov, Dmitry, Coleman, Matthew, Li, Xiao-Dan, Frank, Matthias, and Pedrini, Bill. Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals. United Kingdom: N. p., 2019. Web. doi:10.1107/S2052252518014641.
Casadei, Cecilia M., Nass, Karol, Barty, Anton, Hunter, Mark S., Padeste, Celestino, Tsai, Ching-Ju, Boutet, Sébastien, Messerschmidt, Marc, Sala, Leonardo, Williams, Garth J., Ozerov, Dmitry, Coleman, Matthew, Li, Xiao-Dan, Frank, Matthias, & Pedrini, Bill. Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals. United Kingdom. doi:10.1107/S2052252518014641.
Casadei, Cecilia M., Nass, Karol, Barty, Anton, Hunter, Mark S., Padeste, Celestino, Tsai, Ching-Ju, Boutet, Sébastien, Messerschmidt, Marc, Sala, Leonardo, Williams, Garth J., Ozerov, Dmitry, Coleman, Matthew, Li, Xiao-Dan, Frank, Matthias, and Pedrini, Bill. Tue . "Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals". United Kingdom. doi:10.1107/S2052252518014641.
@article{osti_1481810,
title = {Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals},
author = {Casadei, Cecilia M. and Nass, Karol and Barty, Anton and Hunter, Mark S. and Padeste, Celestino and Tsai, Ching-Ju and Boutet, Sébastien and Messerschmidt, Marc and Sala, Leonardo and Williams, Garth J. and Ozerov, Dmitry and Coleman, Matthew and Li, Xiao-Dan and Frank, Matthias and Pedrini, Bill},
abstractNote = {Serial femtosecond crystallography of two-dimensional membrane-protein crystals at X-ray free-electron lasers has the potential to address the dynamics of functionally relevant large-scale motions, which can be sterically hindered in three-dimensional crystals and suppressed in cryocooled samples. In previous work, diffraction data limited to a two-dimensional reciprocal-space slice were evaluated and it was demonstrated that the low intensity of the diffraction signal can be overcome by collecting highly redundant data, thus enhancing the achievable resolution. Here, the application of a newly developed method to analyze diffraction data covering three reciprocal-space dimensions, extracting the reciprocal-space map of the structure-factor amplitudes, is presented. Despite the low resolution and completeness of the data set, it is shown by molecular replacement that the reconstructed amplitudes carry meaningful structural information. Therefore, it appears that these intrinsic limitations in resolution and completeness from two-dimensional crystal diffraction may be overcome by collecting highly redundant data along the three reciprocal-space axes, thus allowing the measurement of large-scale dynamics in pump–probe experiments.},
doi = {10.1107/S2052252518014641},
journal = {IUCrJ},
number = 1,
volume = 6,
place = {United Kingdom},
year = {Tue Jan 01 00:00:00 EST 2019},
month = {Tue Jan 01 00:00:00 EST 2019}
}

Journal Article:
Free Publicly Available Full Text
This content will become publicly available on January 1, 2019
Publisher's Version of Record

Save / Share: