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.
Highlights
Over the past 50 years, macromolecular crystallography has been responsible for solving the structure of 100 000s of proteins
Radiation damage in a micron-sized protein crystal has been examined using a combination of reciprocal space mapping and BCDI techniques
The additional information provided by real-space images of the crystal as it undergoes dehydration and apparently shrinks in the beam aids in the interpretation of the diffraction data where the convolution of reciprocal and real space information can make separating out the various factors contributing to the measured diffraction intensity challenging
Summary
Over the past 50 years, macromolecular crystallography has been responsible for solving the structure of 100 000s of proteins. The proliferation of high intensity, third-generation synchrotron sources has enabled ever higher-resolution structures to be obtained using data collected from smaller and often more imperfect biological crystals.. With an increase in the X-ray flux incident upon the crystal comes an inevitable increase in the radiation-induced structural damage, leading to a rapid loss in diffraction intensity, for the highest resolution data. Radiation damage at synchrotron and laboratory sources induces structural disorder in the crystal which affects the Bragg peaks and leads to an apparent change in unit cell dimensions reducing the probability of solving the protein structure and hindering biological interpretations.
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