Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8648310 | Journal of Structural Biology | 2017 | 13 Pages |
Abstract
Raman spectroscopy can probe the structure and conformations of specific chemical groups within proteins and may thus be used as a technique complementary to X-ray crystallography. This combined approach can be decisive in resolving ambiguities in the interpretation of enzymatic or X-ray induced processes. Here, we present an online Raman setup developed at the European Synchrotron that allows for interleaved Raman spectra acquisition and X-ray diffraction measurements with fast probe exchange and simple alignment while maintaining a high sensitivity over the entire spectral range. This device has been recently employed in the study of a covalent intermediate in the O2-dependent breakdown of uric acid by the cofactor-free enzyme urate oxidase and to monitor its decay induced by X-ray exposure.
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Authors
David von Stetten, Thierry Giraud, Soi Bui, Roberto A. Steiner, François Fihman, Daniele de Sanctis, Antoine Royant,