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    Structural enzymology using X-ray free electron lasers

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    Author
    Kupitz, C; Olmos, JL; Holl, M; Tremblay, L; Pande, K; Pandey, S; Oberthuer, D; Hunter, M; Liang, M; Aquila, A; ...
    Date
    2017-07-01
    Source Title
    Structural Dynamics
    Publisher
    AMER INST PHYSICS
    University of Melbourne Author/s
    Morgan, Andrew
    Affiliation
    School of Physics
    Metadata
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    Document Type
    Journal Article
    Citations
    Kupitz, C., Olmos, J. L., Holl, M., Tremblay, L., Pande, K., Pandey, S., Oberthuer, D., Hunter, M., Liang, M., Aquila, A., Tenboer, J., Calvey, G., Katz, A., Chen, Y., Wiedorn, M. O., Knoska, J., Meents, A., Majriani, V., Norwood, T. ,... Schmidt, M. (2017). Structural enzymology using X-ray free electron lasers. STRUCTURAL DYNAMICS-US, 4 (4), https://doi.org/10.1063/1.4972069.
    Access Status
    Open Access
    URI
    http://hdl.handle.net/11343/254984
    DOI
    10.1063/1.4972069
    Abstract
    Mix-and-inject serial crystallography (MISC) is a technique designed to image enzyme catalyzed reactions in which small protein crystals are mixed with a substrate just prior to being probed by an X-ray pulse. This approach offers several advantages over flow cell studies. It provides (i) room temperature structures at near atomic resolution, (ii) time resolution ranging from microseconds to seconds, and (iii) convenient reaction initiation. It outruns radiation damage by using femtosecond X-ray pulses allowing damage and chemistry to be separated. Here, we demonstrate that MISC is feasible at an X-ray free electron laser by studying the reaction of M. tuberculosis ß-lactamase microcrystals with ceftriaxone antibiotic solution. Electron density maps of the apo-ß-lactamase and of the ceftriaxone bound form were obtained at 2.8 Å and 2.4 Å resolution, respectively. These results pave the way to study cyclic and non-cyclic reactions and represent a new field of time-resolved structural dynamics for numerous substrate-triggered biological reactions.

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