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Title: Serial snapshot crystallography for materials science with SwissFEL

Abstract

New opportunities for studying (sub)microcrystalline materials with small unit cells, both organic and inorganic, will open up when the X-ray free electron laser (XFEL) presently being constructed in Switzerland (SwissFEL) comes online in 2017. Our synchrotron-based experiments mimicking the 4%-energy-bandpass mode of the SwissFEL beam show that it will be possible to record a diffraction pattern of up to 10 randomly oriented crystals in a single snapshot, to index the resulting reflections, and to extract their intensities reliably. The crystals are destroyed with each XFEL pulse, but by combining snapshots from several sets of crystals, a complete set of data can be assembled, and crystal structures of materials that are difficult to analyze otherwise will become accessible. Even with a single shot, at least a partial analysis of the crystal structure will be possible, and with 10–50 femtosecond pulses, this offers tantalizing possibilities for time-resolved studies.

Authors:
 [1];  [1];  [1];  [2];  [3];  [4];  [1]
  1. Laboratory of Crystallography, ETH Zurich (Switzerland)
  2. Lawrence Berkeley National Lab., CA (United States)
  3. European Synchrotron Radiation Facility, Grenoble (France)
  4. SwissFEL, Paul Scherrer Institut, Villigen PSI (Switzerland)
Publication Date:
Research Org.:
Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Basic Energy Sciences (BES) (SC-22)
OSTI Identifier:
1209942
Grant/Contract Number:
AC02-05CH11231
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
IUCrJ
Additional Journal Information:
Journal Volume: 2; Journal Issue: 3; Journal ID: ISSN 2052-2525
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY

Citation Formats

Dejoie, Catherine, Smeets, Stef, Baerlocher, Christian, Tamura, Nobumichi, Pattison, Philip, Abela, Rafael, and McCusker, Lynne B. Serial snapshot crystallography for materials science with SwissFEL. United States: N. p., 2015. Web. doi:10.1107/S2052252515006740.
Dejoie, Catherine, Smeets, Stef, Baerlocher, Christian, Tamura, Nobumichi, Pattison, Philip, Abela, Rafael, & McCusker, Lynne B. Serial snapshot crystallography for materials science with SwissFEL. United States. doi:10.1107/S2052252515006740.
Dejoie, Catherine, Smeets, Stef, Baerlocher, Christian, Tamura, Nobumichi, Pattison, Philip, Abela, Rafael, and McCusker, Lynne B. Tue . "Serial snapshot crystallography for materials science with SwissFEL". United States. doi:10.1107/S2052252515006740. https://www.osti.gov/servlets/purl/1209942.
@article{osti_1209942,
title = {Serial snapshot crystallography for materials science with SwissFEL},
author = {Dejoie, Catherine and Smeets, Stef and Baerlocher, Christian and Tamura, Nobumichi and Pattison, Philip and Abela, Rafael and McCusker, Lynne B.},
abstractNote = {New opportunities for studying (sub)microcrystalline materials with small unit cells, both organic and inorganic, will open up when the X-ray free electron laser (XFEL) presently being constructed in Switzerland (SwissFEL) comes online in 2017. Our synchrotron-based experiments mimicking the 4%-energy-bandpass mode of the SwissFEL beam show that it will be possible to record a diffraction pattern of up to 10 randomly oriented crystals in a single snapshot, to index the resulting reflections, and to extract their intensities reliably. The crystals are destroyed with each XFEL pulse, but by combining snapshots from several sets of crystals, a complete set of data can be assembled, and crystal structures of materials that are difficult to analyze otherwise will become accessible. Even with a single shot, at least a partial analysis of the crystal structure will be possible, and with 10–50 femtosecond pulses, this offers tantalizing possibilities for time-resolved studies.},
doi = {10.1107/S2052252515006740},
journal = {IUCrJ},
number = 3,
volume = 2,
place = {United States},
year = {Tue Apr 21 00:00:00 EDT 2015},
month = {Tue Apr 21 00:00:00 EDT 2015}
}

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Free Publicly Available Full Text
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  • Using detailed simulation and analytical models, the exposure time is estimated for serial crystallography, where hydrated laser-aligned proteins are sprayed across a continuous synchrotron beam. The resolution of X-ray diffraction microscopy is limited by the maximum dose that can be delivered prior to sample damage. In the proposed Serial Crystallography method, the damage problem is addressed by distributing the total dose over many identical hydrated macromolecules running continuously in a single-file train across a continuous X-ray beam, and resolution is then limited only by the available fluxes of molecules and X-rays. Orientation of the diffracting molecules is achieved by lasermore » alignment. We evaluate the incident X-ray fluence (energy/area) required to obtain a given resolution from (1) an analytical model, giving the count rate at the maximum scattering angle for a model protein, (2) explicit simulation of diffraction patterns for a GroEL-GroES protein complex, and (3) the frequency cut off of the transfer function following iterative solution of the phase problem, and reconstruction of a density map in the projection approximation. These calculations include counting shot noise and multiple starts of the phasing algorithm. The results indicate the number of proteins needed within the beam at any instant for a given resolution and X-ray flux. We confirm an inverse fourth power dependence of exposure time on resolution, with important implications for all coherent X-ray imaging. We find that multiple single-file protein beams will be needed for sub-nanometer resolution on current third generation synchrotrons, but not on fourth generation designs, where reconstruction of secondary protein structure at a resolution of 7 {angstrom} should be possible with short (below 100 s) exposures.« less