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Title: Bragg coherent diffraction imaging and metrics for radiation damage in protein micro-crystallography

Abstract

The proliferation of extremely intense synchrotron sources has enabled ever higher-resolution structures to be obtained using data collected from smaller and often more imperfect biological crystals. Synchrotron beamlines now exist that are capable of measuring data from single crystals that are just a few micrometres in size. This provides renewed motivation to study and understand the radiation damage behaviour of small protein crystals. Reciprocal-space mapping and Bragg coherent diffractive imaging experiments have been performed on cryo-cooled microcrystals of hen egg-white lysozyme as they undergo radiation damage. Several well established metrics, such as intensity-loss and lattice expansion, are applied to the diffraction data and the results are compared with several new metrics that can be extracted from the coherent imaging experiments. Individually some of these metrics are inconclusive. However, combining metrics, the results suggest that radiation damage behaviour in protein micro-crystals differs from that of larger protein crystals and may allow them to continue to diffract for longer. As a result, a possible mechanism to account for these observations is proposed.

Authors:
 [1];  [2];  [2];  [1]; ORCiD logo [2];  [3];  [4];  [5];  [6]; ORCiD logo [6];  [2]
  1. La Trobe Univ., Victoria (Australia); CSIRO Manufacturing Flagship, Parkville (Australia)
  2. La Trobe Univ., Victoria (Australia)
  3. SLAC National Accelerator Lab., Menlo Park, CA (United States); Deutsches Elektronen-Synchrotron (DESY), Hamburg (Germany)
  4. Lawrence Berkeley National Lab. (LBNL), Berkeley, CA (United States)
  5. Univ. of Oxford, Oxford (United Kingdom)
  6. Argonne National Lab. (ANL), Argonne, IL (United States)
Publication Date:
Research Org.:
SLAC National Accelerator Lab., Menlo Park, CA (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1348845
Grant/Contract Number:  
AC02-76SF00515
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Journal of Synchrotron Radiation (Online)
Additional Journal Information:
Journal Name: Journal of Synchrotron Radiation (Online); Journal Volume: 24; Journal Issue: 1; Journal ID: ISSN 1600-5775
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
English
Subject:
46 INSTRUMENTATION RELATED TO NUCLEAR SCIENCE AND TECHNOLOGY; radiation damage; dose; protein crystallography; micro-crystallography; Bragg coherent diffractive imaging

Citation Formats

Coughlan, H. D., Darmanin, C., Kirkwood, H. J., Phillips, N. W., Hoxley, D., Clark, J. N., Vine, D. J., Hofmann, F., Harder, R. J., Maxey, E., and Abbey, B. Bragg coherent diffraction imaging and metrics for radiation damage in protein micro-crystallography. United States: N. p., 2017. Web. doi:10.1107/s1600577516017525.
Coughlan, H. D., Darmanin, C., Kirkwood, H. J., Phillips, N. W., Hoxley, D., Clark, J. N., Vine, D. J., Hofmann, F., Harder, R. J., Maxey, E., & Abbey, B. Bragg coherent diffraction imaging and metrics for radiation damage in protein micro-crystallography. United States. doi:10.1107/s1600577516017525.
Coughlan, H. D., Darmanin, C., Kirkwood, H. J., Phillips, N. W., Hoxley, D., Clark, J. N., Vine, D. J., Hofmann, F., Harder, R. J., Maxey, E., and Abbey, B. Sun . "Bragg coherent diffraction imaging and metrics for radiation damage in protein micro-crystallography". United States. doi:10.1107/s1600577516017525. https://www.osti.gov/servlets/purl/1348845.
@article{osti_1348845,
title = {Bragg coherent diffraction imaging and metrics for radiation damage in protein micro-crystallography},
author = {Coughlan, H. D. and Darmanin, C. and Kirkwood, H. J. and Phillips, N. W. and Hoxley, D. and Clark, J. N. and Vine, D. J. and Hofmann, F. and Harder, R. J. and Maxey, E. and Abbey, B.},
abstractNote = {The proliferation of extremely intense synchrotron sources has enabled ever higher-resolution structures to be obtained using data collected from smaller and often more imperfect biological crystals. Synchrotron beamlines now exist that are capable of measuring data from single crystals that are just a few micrometres in size. This provides renewed motivation to study and understand the radiation damage behaviour of small protein crystals. Reciprocal-space mapping and Bragg coherent diffractive imaging experiments have been performed on cryo-cooled microcrystals of hen egg-white lysozyme as they undergo radiation damage. Several well established metrics, such as intensity-loss and lattice expansion, are applied to the diffraction data and the results are compared with several new metrics that can be extracted from the coherent imaging experiments. Individually some of these metrics are inconclusive. However, combining metrics, the results suggest that radiation damage behaviour in protein micro-crystals differs from that of larger protein crystals and may allow them to continue to diffract for longer. As a result, a possible mechanism to account for these observations is proposed.},
doi = {10.1107/s1600577516017525},
journal = {Journal of Synchrotron Radiation (Online)},
number = 1,
volume = 24,
place = {United States},
year = {Sun Jan 01 00:00:00 EST 2017},
month = {Sun Jan 01 00:00:00 EST 2017}
}

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Cited by: 5 works
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Works referenced in this record:

Room-temperature macromolecular serial crystallography using synchrotron radiation
journal, May 2014

  • Stellato, Francesco; Oberth├╝r, Dominik; Liang, Mengning
  • IUCrJ, Vol. 1, Issue 4, p. 204-212
  • DOI: 10.1107/S2052252514010070