dc.contributor.author | Beyerlein, Kenneth R. | |
dc.contributor.author | Dierksmeyer, Dennis | |
dc.contributor.author | Mariani, Valerio | |
dc.contributor.author | Kuhn, Manuela | |
dc.contributor.author | Sarrou, Iosifina | |
dc.contributor.author | Ottaviano, Angelica | |
dc.contributor.author | Awel, Salah | |
dc.contributor.author | Knoska, Juraj | |
dc.contributor.author | Fuglerud, Silje Skeide | |
dc.contributor.author | Jönsson, Olof | |
dc.contributor.author | Stern, Stephan | |
dc.contributor.author | Wiedorn, Max O. | |
dc.contributor.author | Yefanov, Oleksandr | |
dc.contributor.author | Adriano, Luigi | |
dc.contributor.author | Bean, Richard | |
dc.contributor.author | Burkhardt, Anja | |
dc.contributor.author | Fischer, Pontus | |
dc.contributor.author | Heymann, Michael | |
dc.contributor.author | Horke, Daniel A. | |
dc.contributor.author | Jungnickel, Katharina E.J. | |
dc.contributor.author | Kovaleva, Elena | |
dc.contributor.author | Lorbeer, Olga | |
dc.contributor.author | Metz, Markus | |
dc.contributor.author | Meyer, Jan | |
dc.contributor.author | Morgan, Andrew | |
dc.contributor.author | Pande, Kanupriya | |
dc.contributor.author | Panneerselvam, Saravanan | |
dc.contributor.author | Seuring, Carolin | |
dc.contributor.author | Tolstikova, Aleksandra | |
dc.contributor.author | Lieske, Julia | |
dc.contributor.author | Aplin, Steve | |
dc.contributor.author | Roessle, Manfred | |
dc.contributor.author | White, Thomas A. | |
dc.contributor.author | Chapman, Henry N. | |
dc.contributor.author | Meents, Alke | |
dc.contributor.author | Oberthuer, Dominik | |
dc.date.accessioned | 2018-08-22T08:06:37Z | |
dc.date.available | 2018-08-22T08:06:37Z | |
dc.date.created | 2018-01-08T15:54:23Z | |
dc.date.issued | 2017 | |
dc.identifier.citation | IUCrJ. 2017, 4 (6), 769-777. | nb_NO |
dc.identifier.issn | 2052-2525 | |
dc.identifier.uri | http://hdl.handle.net/11250/2558782 | |
dc.description.abstract | Unravelling 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. | nb_NO |
dc.language.iso | eng | nb_NO |
dc.publisher | International Union of Crystallography | nb_NO |
dc.rights | Navngivelse 4.0 Internasjonal | * |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/deed.no | * |
dc.title | Mix-and-diffuse serial synchrotron crystallography | nb_NO |
dc.type | Journal article | nb_NO |
dc.type | Peer reviewed | nb_NO |
dc.description.version | publishedVersion | nb_NO |
dc.source.pagenumber | 769-777 | nb_NO |
dc.source.volume | 4 | nb_NO |
dc.source.journal | IUCrJ | nb_NO |
dc.source.issue | 6 | nb_NO |
dc.identifier.doi | 10.1107/S2052252517013124 | |
dc.identifier.cristin | 1538052 | |
dc.description.localcode | This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. | nb_NO |
cristin.unitcode | 194,66,20,0 | |
cristin.unitname | Institutt for fysikk | |
cristin.ispublished | true | |
cristin.fulltext | original | |
cristin.qualitycode | 1 | |