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

By Cecilia M. Casadei, Karol Nass, Anton Barty, Mark S. Hunter1, Celestino Padeste, Ching-Ju Tsai, Sébastien Boutet, Marc Messerschmidt2, Leonardo Sala, Garth J. Williams, Dmitry Ozerov, Matthew Coleman3, Xiao-Dan Li, Matthias Frank4, Bill Pedrini

1. SLAC National Accelerator Laboratory 2. Arizona State University 3. Radiation Oncology, Cancer Center 4. Lawrence Livermore National Laboratory

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Category

BioXFEL Publications

Published on

Type

journal-article

Author

Cecilia M. Casadei and Karol Nass and Anton Barty and Mark S. Hunter and Celestino Padeste and Ching-Ju Tsai and Sébastien Boutet and Marc Messerschmidt and Leonardo Sala and Garth J. Williams and Dmitry Ozerov and Matthew Coleman and Xiao-Dan Li and Matthias Frank and Bill Pedrini

Citation

Casadei, C.M. et al., 2019. Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals. IUCrJ, 6(1). Available at: http://dx.doi.org/10.1107/s2052252518014641.

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.

DOI

http://dx.doi.org/10.1107/s2052252518014641

Funding

NSF-STC Biology with X-ray Lasers (NSF-1231306)