Structure-factor amplitude reconstruction from serial femtosecond crystallography of two-dimensional membrane-protein crystals.
- Casadei CM Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.
- Nass K Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.
- Barty A Center for Free-Electron Laser Science, DESY, Notkestrasse 85, 22607 Hamburg, Germany.
- Hunter MS Lawrence Livermore National Laboratory, 7000 East Avenue, Livermore, CA 94550, USA.
- Padeste C Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.
- Tsai CJ Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.
- Boutet S Linac Coherent Light Source, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.
- Messerschmidt M Linac Coherent Light Source, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.
- Sala L Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.
- Williams GJ Linac Coherent Light Source, 2575 Sand Hill Road, Menlo Park, CA 94025, USA.
- Ozerov D Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.
- Coleman M Lawrence Livermore National Laboratory, 7000 East Avenue, Livermore, CA 94550, USA.
- Li XD Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.
- Frank M Lawrence Livermore National Laboratory, 7000 East Avenue, Livermore, CA 94550, USA.
- Pedrini B Paul Scherrer Institute, 5232 Villigen PSI, Switzerland.
- 2019-02-05
Published in:
- IUCrJ. - 2019
English
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.
- Language
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- English
- Open access status
- gold
- Identifiers
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- DOI 10.1107/S2052252518014641
- PMID 30713701
- Persistent URL
- https://sonar.ch/global/documents/1090
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