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dc.contributor.authorBeyerlein, KR
dc.contributor.authorDierksmeyer, D
dc.contributor.authorMariani, V
dc.contributor.authorKuhn, M
dc.contributor.authorSarrou, I
dc.contributor.authorOttaviano, A
dc.contributor.authorAwel, S
dc.contributor.authorKnoska, J
dc.contributor.authorFuglerud, S
dc.contributor.authorJonsson, O
dc.contributor.authorStern, S
dc.contributor.authorWiedorn, MO
dc.contributor.authorYefanov, O
dc.contributor.authorAdriano, L
dc.contributor.authorBean, R
dc.contributor.authorBurkhardt, A
dc.contributor.authorFischer, P
dc.contributor.authorHeymann, M
dc.contributor.authorHorke, DA
dc.contributor.authorJungnickel, KEJ
dc.contributor.authorKovaleva, E
dc.contributor.authorLorbeer, O
dc.contributor.authorMetz, M
dc.contributor.authorMeyer, J
dc.contributor.authorMorgan, A
dc.contributor.authorPande, K
dc.contributor.authorPanneerselvam, S
dc.contributor.authorSeuring, C
dc.contributor.authorTolstikova, A
dc.contributor.authorLieske, J
dc.contributor.authorAplin, S
dc.contributor.authorRoessle, M
dc.contributor.authorWhite, TA
dc.contributor.authorChapman, HN
dc.contributor.authorMeents, A
dc.contributor.authorOberthuer, D
dc.date.accessioned2020-12-10T01:31:51Z
dc.date.available2020-12-10T01:31:51Z
dc.date.issued2017-11-01
dc.identifierpii: ec5004
dc.identifier.citationBeyerlein, K. R., Dierksmeyer, D., Mariani, V., Kuhn, M., Sarrou, I., Ottaviano, A., Awel, S., Knoska, J., Fuglerud, S., Jonsson, O., Stern, S., Wiedorn, M. O., Yefanov, O., Adriano, L., Bean, R., Burkhardt, A., Fischer, P., Heymann, M., Horke, D. A. ,... Oberthuer, D. (2017). Mix-and-diffuse serial synchrotron crystallography. IUCRJ, 4 (Pt 6), pp.769-777. https://doi.org/10.1107/S2052252517013124.
dc.identifier.issn2052-2525
dc.identifier.urihttp://hdl.handle.net/11343/253728
dc.description.abstractUnravelling the interaction of biological macromolecules with ligands and substrates at high spatial and temporal resolution remains a major challenge in structural biology. The development of serial crystallography methods at X-ray free-electron lasers and subsequently at synchrotron light sources allows new approaches to tackle this challenge. Here, a new polyimide tape drive designed for mix-and-diffuse serial crystallography experiments is reported. The structure of lysozyme bound by the competitive inhibitor chitotriose was determined using this device in combination with microfluidic mixers. The electron densities obtained from mixing times of 2 and 50 s show clear binding of chitotriose to the enzyme at a high level of detail. The success of this approach shows the potential for high-throughput drug screening and even structural enzymology on short timescales at bright synchrotron light sources.
dc.languageEnglish
dc.publisherINT UNION CRYSTALLOGRAPHY
dc.rights.urihttps://creativecommons.org/licenses/by/4.0
dc.titleMix-and-diffuse serial synchrotron crystallography
dc.typeJournal Article
dc.identifier.doi10.1107/S2052252517013124
melbourne.affiliation.departmentSchool of Physics
melbourne.source.titleIUCrJ
melbourne.source.volume4
melbourne.source.issuePt 6
melbourne.source.pages769-777
dc.rights.licenseCC BY
melbourne.elementsid1326199
melbourne.contributor.authorMorgan, Andrew
dc.identifier.eissn2052-2525
melbourne.accessrightsOpen Access


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