Abstract
The recent advent of intense, polychromatic, pulsed synchrotron x-ray sources has prompted a re-examination of the Laue diffraction technique, particularly as applied to crystals of proteins and other macromolecules. This article reviews briefly the main aspects of the Laue technique, and how it may be applied to the general area of time-resolved crystallography. Applications have as their goal the elucidation of the structure of short-lived intermediates in such processes as enzymatic catalysis, ligand binding and release, and protein folding and unfolding. Knowledge of the structure of such intermediates is critical to a full understanding of molecular mechanisms of action, yet they are inaccessible to conventional x-ray techniques since their lifetimes are typically very much less than one second.
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Moffat, K., Bilderback, D., Schildkamp, W., Szebenyi, D., Teng, Ty. (1989). Laue Photography from Protein Crystals. In: Sweet, R.M., Woodhead, A.D. (eds) Synchrotron Radiation in Structural Biology. Basic Life Sciences, vol 51. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8041-2_29
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DOI: https://doi.org/10.1007/978-1-4684-8041-2_29
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