Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy

Demet Kekilli, Florian S. N. Dworkowski, Guillaume Pompidor, Martin R. Fuchs, Colin R. Andrew, Svetlana Antonyuk, Richard W. Strange, Robert R. Eady, S. Samar Hasnain, Michael A. Hough
  • Acta Crystallographica Section D Biological Crystallography, April 2014, International Union of Crystallography
  • DOI: 10.1107/s1399004714004039

Fingerprinting crystal structures with Raman spectroscopy

What is it about?

X-ray crystallography is a vital means of understanding protein structure. It is important to ensure that the structures generated by this method represent the true state of the protein in the organism and also that the X-rays have not changed or damaged the protein. In this paper we used a spectroscopic method to obtain 'fingerprints' for different states of the protein. This approach allows us to identify the starting state of the protein as well as to monitor any changes due to X-ray exposure

Why is it important?

This work, carried out in collaboration with Swiss Light Source scientists shows the use of Raman spectroscopy as an efficient fingerprinting tool. It has the potential to be applied at other synchrotrons for structure validation and to maximise the information content of combined spectroscopic-crystallographic experiments.

The following have contributed to this page: Dr Michael A Hough and Dr Florian Sven Nico Dworkowski