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Combining X‐ray and neutron crystallography with spectroscopy
Author(s) -
Kwon Hanna,
Smith Oliver,
Raven Emma Lloyd,
Moody Peter C. E.
Publication year - 2017
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798316016314
Subject(s) - crystallography , spectroscopy , x ray , crystal (programming language) , neutron , x ray spectroscopy , chemistry , crystal structure , scattering , electron , physics , optics , nuclear physics , quantum mechanics , computer science , programming language
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.