Feasibility studies of freeze-trapping of structural intermediates in proteins using cryo neutron crystallography on instrument D19
We propose to use the recently tested D19 cryostream system to investigate the possibility to cryo-trap structural intermediates in enzyme reactions. Although cryo-trapping is a commonly-used technique in X-ray crystallography, as far as neutron crystallography is concerned it would be amongst the first studies of this type. Neutron diffraction would bring crucial insights into such biomolecular processes, allowing hydrogen transfer and protonation states to be observed. Intermediates of systems like Xylose Isomerase have been studied using D19 and allowed the determination of hydrogen transfer mechanism during the reaction. This study was carried out at room temperature and necessitated the use of several compounds representing each stage of the reaction. The development of cryo-trapping in neutron crystallography would open-up huge avenues for future college 8 proposals. We therefore suggest using a series of model enzyme-systems known to grow large crystals suitable for neutron diffraction, to develop a reliable method for cryo-trapping using D19. Given that it is driven by technical issues rather than biological, this proposal clearly falls within the remit of College 1.
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MOSSOU Estelle; Matthew P. Blakeley; CUYPERS Maxime; FORSYTH Victor Trevor; MASON, Sax A.; MCSWEENEY SEAN and ROMOLI Filippo. (2013). Feasibility studies of freeze-trapping of structural intermediates in proteins using cryo neutron crystallography on instrument D19. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.1-20-33
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