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Acta Crystallogr A. 2010 March 1; 66(Pt 2): 207–219.
Published online 2010 February 18. doi:  10.1107/S0108767309054361
PMCID: PMC2824530

Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches

Abstract

Proteins undergo conformational changes during their biological function. As such, a high-resolution structure of a protein’s resting conformation provides a starting point for elucidating its reaction mechanism, but provides no direct information concerning the protein’s conformational dynamics. Several X-ray methods have been developed to elucidate those conformational changes that occur during a protein’s reaction, including time-resolved Laue diffraction and intermediate trapping studies on three-dimensional protein crystals, and time-resolved wide-angle X-ray scattering and X-ray absorption studies on proteins in the solution phase. This review emphasizes the scope and limitations of these complementary experimental approaches when seeking to understand protein conformational dynamics. These methods are illustrated using a limited set of examples including myoglobin and haemoglobin in complex with carbon monoxide, the simple light-driven proton pump bacteriorhodopsin, and the superoxide scavenger superoxide reductase. In conclusion, likely future developments of these methods at synchrotron X-ray sources and the potential impact of emerging X-ray free-electron laser facilities are speculated upon.

Keywords: time-resolved diffraction, structural biology, protein structural dynamics, Laue diffraction, kinetic crystallography, WAXS, XAS

Articles from Acta Crystallographica Section A: Foundations of Crystallography are provided here courtesy of International Union of Crystallography