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Combining X-ray and neutron crystallography with spectroscopy.

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journal contribution
posted on 22.03.2017, 14:46 by Hanna Kwon, Oliver Smith, Emma Lloyd Raven, Peter C. E. Moody
X-ray protein crystallography has, through the determination of the three-dimensional structures of enzymes and their complexes, been essential to the understanding of biological chemistry. However, as X-rays are scattered by electrons, the technique has difficulty locating the presence and position of H atoms (and cannot locate H(+) ions), knowledge of which is often crucially important for the understanding of enzyme mechanism. Furthermore, X-ray irradiation, through photoelectronic effects, will perturb the redox state in the crystal. By using single-crystal spectrophotometry, reactions taking place in the crystal can be monitored, either to trap intermediates or follow photoreduction during X-ray data collection. By using neutron crystallography, the positions of H atoms can be located, as it is the nuclei rather than the electrons that scatter neutrons, and the scattering length is not determined by the atomic number. Combining the two techniques allows much greater insight into both reaction mechanism and X-ray-induced photoreduction.


We wish to thank the BBSRC (BB/K015665/1) and Wellcome Trust (WT094104MA) for support and Professor Nigel Scrutton (University of Manchester) for the gift of the expression system for PETN reductase.



Acta crystallographica. Section D, Structural biology, 2017, 73 (Pt 2), pp. 141-147

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/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGY/MBSP Non-Medical Departments/Molecular & Cell Biology


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Acta crystallographica. Section D


International Union of Crystallography



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