Radiation damage in a micron-sized protein crystal studied via reciprocal space mapping and Bragg coherent diffractive imaging

Radiation damage in a micron-sized protein crystal studied via reciprocal space mapping and Bragg coherent diffractive imaging

For laboratory and synchrotron based X-ray sources, radiation damage has posed a significant barrier to obtaining high-resolution structural data from biological macromolecules. The problem is particularly acute for micron-sized crystals where the weaker signal often ne...

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Main Authors: H. D. Coughlan, C. Darmanin, N. W. Phillips, F. Hofmann, J. N. Clark, R. J. Harder, D. J. Vine, B. Abbey
Format: Article
Language:English
Published: AIP Publishing LLC and ACA 2015-07-01
Series:Structural Dynamics
Online Access:http://dx.doi.org/10.1063/1.4919641
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spelling doaj-fc2ca7c4201446439cf9ca408771c3262020-11-24T23:29:15ZengAIP Publishing LLC and ACAStructural Dynamics2329-77782015-07-0124041704041704-1310.1063/1.4919641005591SDYRadiation damage in a micron-sized protein crystal studied via reciprocal space mapping and Bragg coherent diffractive imagingH. D. Coughlan0C. Darmanin1N. W. Phillips2F. Hofmann3J. N. Clark4R. J. Harder5D. J. Vine6B. Abbey7 Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe University, Melbourne 3086, Australia Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe University, Melbourne 3086, Australia Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe University, Melbourne 3086, Australia Department of Engineering Science, University of Oxford, Oxford OX1 3PJ, United Kingdom Stanford PULSE Institute, SLAC National Accelerator Laboratory, Menlo Park, California 94025, USA Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois 60439, USA Advanced Photon Source, Argonne National Laboratory, Argonne, Illinois 60439, USA Australian Research Council Centre of Excellence in Advanced Molecular Imaging, Department of Chemistry and Physics, La Trobe University, Melbourne 3086, AustraliaFor laboratory and synchrotron based X-ray sources, radiation damage has posed a significant barrier to obtaining high-resolution structural data from biological macromolecules. The problem is particularly acute for micron-sized crystals where the weaker signal often necessitates the use of higher intensity beams to obtain the relevant data. Here, we employ a combination of techniques, including Bragg coherent diffractive imaging to characterise the radiation induced damage in a micron-sized protein crystal over time. The approach we adopt here could help screen for potential protein crystal candidates for measurement at X-ray free election laser sources.http://dx.doi.org/10.1063/1.4919641
collection DOAJ
language English
format Article
sources DOAJ
author H. D. Coughlan
C. Darmanin
N. W. Phillips
F. Hofmann
J. N. Clark
R. J. Harder
D. J. Vine
B. Abbey
spellingShingle H. D. Coughlan
C. Darmanin
N. W. Phillips
F. Hofmann
J. N. Clark
R. J. Harder
D. J. Vine
B. Abbey
Radiation damage in a micron-sized protein crystal studied via reciprocal space mapping and Bragg coherent diffractive imaging
Structural Dynamics
author_facet H. D. Coughlan
C. Darmanin
N. W. Phillips
F. Hofmann
J. N. Clark
R. J. Harder
D. J. Vine
B. Abbey
author_sort H. D. Coughlan
title Radiation damage in a micron-sized protein crystal studied via reciprocal space mapping and Bragg coherent diffractive imaging
title_short Radiation damage in a micron-sized protein crystal studied via reciprocal space mapping and Bragg coherent diffractive imaging
title_full Radiation damage in a micron-sized protein crystal studied via reciprocal space mapping and Bragg coherent diffractive imaging
title_fullStr Radiation damage in a micron-sized protein crystal studied via reciprocal space mapping and Bragg coherent diffractive imaging
title_full_unstemmed Radiation damage in a micron-sized protein crystal studied via reciprocal space mapping and Bragg coherent diffractive imaging
title_sort radiation damage in a micron-sized protein crystal studied via reciprocal space mapping and bragg coherent diffractive imaging
publisher AIP Publishing LLC and ACA
series Structural Dynamics
issn 2329-7778
publishDate 2015-07-01
description For laboratory and synchrotron based X-ray sources, radiation damage has posed a significant barrier to obtaining high-resolution structural data from biological macromolecules. The problem is particularly acute for micron-sized crystals where the weaker signal often necessitates the use of higher intensity beams to obtain the relevant data. Here, we employ a combination of techniques, including Bragg coherent diffractive imaging to characterise the radiation induced damage in a micron-sized protein crystal over time. The approach we adopt here could help screen for potential protein crystal candidates for measurement at X-ray free election laser sources.
url http://dx.doi.org/10.1063/1.4919641
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AT nwphillips radiationdamageinamicronsizedproteincrystalstudiedviareciprocalspacemappingandbraggcoherentdiffractiveimaging
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