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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Bibliographic Details
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
Description
Summary: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.
ISSN:2329-7778

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