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Nature Methods 5, 881–886 (1 October 2008) | doi:10.1038/nmeth.1255

Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering

Marco Cammarata , Matteo Levantino , Friedrich Schotte , Philip A Anfinrud , Friederike Ewald , Jungkweon Choi , Antonio Cupane , Michael Wulff & Hyotcherl Ihee

We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.