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.
Original language | English |
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Pages (from-to) | 124-127 |
Journal | Journal of Structural Biology |
Volume | 200 |
Issue number | 2 |
Early online date | 16 Oct 2017 |
DOIs | |
Publication status | E-pub ahead of print - 16 Oct 2017 |
Keywords
- Raman spectroscopy
- Macromolecular crystallography
- Diffraction-complementary technique
- Kinetic crystallography
- Radiation damage