Synchrotron Powder Diffraction Study of Radiation Damage in Langmuir Blodgett Nanotemplate Crystallised Protein
Jonathan P. Wright1, Eugenia Pechkova2 & Claudio Nicolini3 Show affiliations
- ESRF, France
- LNB-DIMES University of Genova, Italy
- Nanoworld Institute, Italy
American Journal of Biochemistry and Biotechnology, Volume 10, Issue 3, pp. 162–168 · doi.org/10.3844/ajbbsp.2014.162.168
Abstract
Polycrystalline samples of lysozyme were prepared with and without a Langmuir-Blodgett (LB) thin film template via both the hanging drop method and batch crystallisation. Powder diffraction methods are used to compare these samples and to measure their resistance to radiation damage at room temperature. The X-ray induced amorphisation of the samples was followed as a function of time and it was shown that diffraction does not entirely disappear even at very long exposure times. Two distinct kinetic timescales are evident suggesting that early and late stage processes are quite different. Radiation damage was also shown to be localized in the sample in the region where the beam impinges.
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Wright, J. P., Pechkova, E. & Nicolini, C. (2014). Synchrotron Powder Diffraction Study of Radiation Damage in Langmuir Blodgett Nanotemplate Crystallised Protein. American Journal of Biochemistry and Biotechnology, 10(3), 162–168. https://doi.org/10.3844/ajbbsp.2014.162.168
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