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Our research concentrates on the application of synchrotron radiation techniques to dynamic X-ray diffraction studies of macromolecules.
For the past 60 years, crystallographers have used monochromatic X-rays almost exclusively, that yield a static, time- and space-average structure of crystals of both small and large molecules. The time-average is taken over the duration of the X-ray exposure, which is typically several hours with laboratory sources; and the space-average over all the molecules in the crystal, typically 1013 in number. With the advent of extremely intense, polychromatic, pulsed synchrotron X-ray sources, the X-ray exposure times have dropped dramatically to the millisecond time range and, in special cases, to 150 picoseconds. That is, exposure times are now comparable with the lifetime of biochemical intermediates in such fundamental processes as enzyme catalysis, ligand-binding and release, and photocycling in light-sensitive systems. The question then arises: Can we generate such intermediates in the crystal and follow the evolution of their tertiary structures as the reaction proceeds, through observation of changes in the X-ray diffraction intensities? Attacking the question requires suitable X-ray optics, cameras, detectors, computer software, and crystallographic theory, which can then be applied to studying crystals that respond to photoactivation, to a temperature or pressure jump, or to diffusion into the crystal of a substrate or reactant.
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bioRxiv : the preprint server for biology (2023)
bioRxiv : the preprint server for biologyno. 11 (2023): e1011048-e1011048
Nicole C Woitowich,Andrei S Halavaty, Patricia Waltz,Christopher Kupitz, Joseph Valera,Gregory Tracy,Kevin D Gallagher,Elin Claesson,Takanori Nakane,Suraj Pandey,Garrett Nelson,Rie Tanaka,
IUCrJno. Pt 5 (2018): 619-634
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