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

Structural Dynamics
H D CoughlanB Abbey

Abstract

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.

References

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Citations

Dec 24, 2016·Journal of Synchrotron Radiation·H D CoughlanB Abbey
Dec 25, 2015·Journal of Synchrotron Radiation·Colin NaveDavid Ian Stuart
Sep 2, 2017·Journal of Synchrotron Radiation·Felix HofmannBrian Abbey
Apr 2, 2021·ACS Nano·Rafael A VicentePablo S Fernández

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Methods Mentioned

BETA
X-ray
coherent diffraction
confocal
scanning electron microscopy
imaging techniques

Software Mentioned

XRT
MATLAB
RAAR
BCDI
RADDOSE
ImageJ

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