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dc.contributor.authorKupitz, C
dc.contributor.authorOlmos, JL
dc.contributor.authorHoll, M
dc.contributor.authorTremblay, L
dc.contributor.authorPande, K
dc.contributor.authorPandey, S
dc.contributor.authorOberthuer, D
dc.contributor.authorHunter, M
dc.contributor.authorLiang, M
dc.contributor.authorAquila, A
dc.contributor.authorTenboer, J
dc.contributor.authorCalvey, G
dc.contributor.authorKatz, A
dc.contributor.authorChen, Y
dc.contributor.authorWiedorn, MO
dc.contributor.authorKnoska, J
dc.contributor.authorMeents, A
dc.contributor.authorMajriani, V
dc.contributor.authorNorwood, T
dc.contributor.authorPoudyal, I
dc.contributor.authorGrant, T
dc.contributor.authorMiller, MD
dc.contributor.authorXu, W
dc.contributor.authorTolstikova, A
dc.contributor.authorMorgan, A
dc.contributor.authorMetz, M
dc.contributor.authorMartin-Garcia, JM
dc.contributor.authorZook, JD
dc.contributor.authorRoy-Chowdhury, S
dc.contributor.authorCoe, J
dc.contributor.authorNagaratnam, N
dc.contributor.authorMeza, D
dc.contributor.authorFromme, R
dc.contributor.authorBasu, S
dc.contributor.authorFrank, M
dc.contributor.authorWhite, T
dc.contributor.authorBarty, A
dc.contributor.authorBajt, S
dc.contributor.authorYefanov, O
dc.contributor.authorChapman, HN
dc.contributor.authorZatsepin, N
dc.contributor.authorNelson, G
dc.contributor.authorWeierstall, U
dc.contributor.authorSpence, J
dc.contributor.authorSchwander, P
dc.contributor.authorPollack, L
dc.contributor.authorFromme, P
dc.contributor.authorOurmazd, A
dc.contributor.authorPhillips, GN
dc.contributor.authorSchmidt, M
dc.date.accessioned2020-12-17T03:40:37Z
dc.date.available2020-12-17T03:40:37Z
dc.date.issued2017-07-01
dc.identifierpii: 002795SDY
dc.identifier.citationKupitz, 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.
dc.identifier.issn2329-7778
dc.identifier.urihttp://hdl.handle.net/11343/254984
dc.description.abstractMix-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.
dc.languageEnglish
dc.publisherAMER INST PHYSICS
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleStructural enzymology using X-ray free electron lasers
dc.typeJournal Article
dc.identifier.doi10.1063/1.4972069
melbourne.affiliation.departmentSchool of Physics
melbourne.source.titleStructural Dynamics
melbourne.source.volume4
melbourne.source.issue4
dc.rights.licenseCC BY
melbourne.elementsid1326202
melbourne.contributor.authorMorgan, Andrew
dc.identifier.eissn2329-7778
melbourne.accessrightsOpen Access


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