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Instruments / Technical Area	Publication Details	Published
I03-Macromolecular Crystallography	Megahertz serial crystallography Max O. Wiedorn , Dominik Oberthuer , Richard Bean , Robin Schubert , Nadine Werner , Brian Abbey , Martin Aepfelbacher , Luigi Adriano , Aschkan Allahgholi , Nasser Al-qudami , Jakob Andreasson , Steve Aplin , Salah Awel , Kartik Ayyer , Saša Bajt , Imrich Barák , Sadia Bari , Johan Bielecki , Sabine Botha , Djelloul Boukhelef , Wolfgang Brehm , Sandor Brockhauser , Igor Cheviakov , Matthew A. Coleman , Francisco Cruz-mazo , Cyril Danilevski , Connie Darmanin , R. Bruce Doak , Martin Domaracky , Katerina Dörner , Yang Du , Hans Fangohr , Holger Fleckenstein , Matthias Frank , Petra Fromme , Alfonso M. Gañán-calvo , Yaroslav Gevorkov , Klaus Giewekemeyer , Helen Mary Ginn , Heinz Graafsma , Rita Graceffa , Dominic Greiffenberg , Lars Gumprecht , Peter Göttlicher , Janos Hajdu , Steffen Hauf , Michael Heymann , Susannah Holmes , Daniel A. Horke , Mark S. Hunter , Siegfried Imlau , Alexander Kaukher , Yoonhee Kim , Alexander Klyuev , Juraj Knoška , Bostjan Kobe , Manuela Kuhn , Christopher Kupitz , Jochen Küpper , Janine Mia Lahey-rudolph , Torsten Laurus , Karoline Le Cong , Romain Letrun , P. Lourdu Xavier , Luis Maia , Filipe R. N. C. Maia , Valerio Mariani , Marc Messerschmidt , Markus Metz , Davide Mezza , Thomas Michelat , Grant Mills , Diana C. F. Monteiro , Andrew Morgan , Kerstin Mühlig , Anna Munke , Astrid Münnich , Julia Nette , Keith A. Nugent , Theresa Nuguid , Allen M. Orville , Suraj Pandey , Gisel Pena , Pablo Villanueva-perez , Jennifer Poehlsen , Gianpietro Previtali , Lars Redecke , Winnie Maria Riekehr , Holger Rohde , Adam Round , Tatiana Safenreiter , Iosifina Sarrou , Tokushi Sato , Marius Schmidt , Bernd Schmitt , Robert Schönherr , Joachim Schulz , Jonas A. Sellberg , M. Marvin Seibert , Carolin Seuring , Megan L. Shelby , Robert L. Shoeman , Marcin Sikorski , Alessandro Silenzi , Claudiu A. Stan , Xintian Shi , Stephan Stern , Jola Sztuk-dambietz , Janusz Szuba , Aleksandra Tolstikova , Martin Trebbin , Ulrich Trunk , Patrik Vagovic , Thomas Ve , Britta Weinhausen , Thomas A. White , Krzysztof Wrona , Chen Xu , Oleksandr Yefanov , Nadia Zatsepin , Jiaguo Zhang , Markus Perbandt , Adrian P. Mancuso , Christian Betzel , Henry Chapman , Anton Barty Nature Communications 9 DOI: 10.1038/s41467-018-06156-7 Open Access Show Abstract ▼ Abstract: The new European X-ray Free-Electron Laser is the first X-ray free-electron laser capable of delivering X-ray pulses with a megahertz inter-pulse spacing, more than four orders of magnitude higher than previously possible. However, to date, it has been unclear whether it would indeed be possible to measure high-quality diffraction data at megahertz pulse repetition rates. Here, we show that high-quality structures can indeed be obtained using currently available operating conditions at the European XFEL. We present two complete data sets, one from the well-known model system lysozyme and the other from a so far unknown complex of a β-lactamase from K. pneumoniae involved in antibiotic resistance. This result opens up megahertz serial femtosecond crystallography (SFX) as a tool for reliable structure determination, substrate screening and the efficient measurement of the evolution and dynamics of molecular structures using megahertz repetition rate pulses available at this new class of X-ray laser source.	Oct 2018
	Femtosecond X-ray coherent diffraction of aligned amyloid fibrils on low background graphene Carolin Seuring , Kartik Ayyer , Eleftheria Filippaki , Miriam Barthelmess , Jean-nicolas Longchamp , Philippe Ringler , Tommaso Pardini , David H. Wojtas , Matthew A. Coleman , Katerina Dörner , Silje Fuglerud , Greger Hammarin , Birgit Habenstein , Annette E. Langkilde , Antoine Loquet , Alke Meents , Roland Riek , Henning Stahlberg , Sébastien Boutet , Mark S. Hunter , Jason Koglin , Mengning Liang , Helen M. Ginn , Rick P. Millane , Matthias Frank , Anton Barty , Henry N. Chapman Nature Communications 9 DOI: 10.1038/s41467-018-04116-9 Open Access Show Abstract ▼ Abstract: Here we present a new approach to diffraction imaging of amyloid fibrils, combining a free-standing graphene support and single nanofocused X-ray pulses of femtosecond duration from an X-ray free-electron laser. Due to the very low background scattering from the graphene support and mutual alignment of filaments, diffraction from tobacco mosaic virus (TMV) filaments and amyloid protofibrils is obtained to 2.7 Å and 2.4 Å resolution in single diffraction patterns, respectively. Some TMV diffraction patterns exhibit asymmetry that indicates the presence of a limited number of axial rotations in the XFEL focus. Signal-to-noise levels from individual diffraction patterns are enhanced using computational alignment and merging, giving patterns that are superior to those obtainable from synchrotron radiation sources. We anticipate that our approach will be a starting point for further investigations into unsolved structures of filaments and other weakly scattering objects.	May 2018
I24-Microfocus Macromolecular Crystallography	Ternary structure reveals mechanism of a membrane diacylglycerol kinase Dianfan Li , Phillip J. Stansfeld , Mark S. P. Sansom , Aaron Keogh , Lutz Vogeley , Nicole Howe , Joseph Lyons , David Aragao , Petra Fromme , Raimund Fromme , Shibom Basu , Ingo Grotjohann , Christopher Kupitz , Kimberley Rendek , Uwe Weierstall , Nadia A. Zatsepin , Vadim Cherezov , Wei Liu , Sateesh Bandaru , Niall J. English , Cornelius Gati , Anton Barty , Oleksandr Yefanov , Henry N. Chapman , Kay Diederichs , Marc Messerschmidt , Sébastien Boutet , Garth J. Williams , M. Marvin Seibert , Martin Caffrey Nature Communications 6 DOI: 10.1038/ncomms10140 Open Access Show Abstract ▼ Abstract: Diacylglycerol kinase catalyses the ATP-dependent conversion of diacylglycerol to phosphatidic acid in the plasma membrane of Escherichia coli. The small size of this integral membrane trimer, which has 121 residues per subunit, means that available protein must be used economically to craft three catalytic and substrate-binding sites centred about the membrane/cytosol interface. How nature has accomplished this extraordinary feat is revealed here in a crystal structure of the kinase captured as a ternary complex with bound lipid substrate and an ATP analogue. Residues, identified as essential for activity by mutagenesis, decorate the active site and are rationalized by the ternary structure. The γ-phosphate of the ATP analogue is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane. A catalytic mechanism for this unique enzyme is proposed. The active site architecture shows clear evidence of having arisen by convergent evolution.	Dec 2015
	Lipidic cubic phase serial millisecond crystallography using synchrotron radiation Przemyslaw Nogly , Daniel James , Dingjie Wang , Thomas A. White , Nadia Zatsepin , Anastasya Shilova , Garrett Nelson , Haiguang Liu , Linda Johansson , Michael Heymann , Kathrin Jaeger , Markus Metz , Cecilia Wickstrand , Wenting Wu , Petra Båth , Peter Berntsen , Dominik Oberthuer , Valerie Panneels , Vadim Cherezov , Isabel Moraes , Henry Chapman , Gebhard Schertler , Richard Neutze , John Spence , Manfred Burghammer , Joerg Standfuss , Uwe Weierstall Iucrj 2, 168 - 176 DOI: 10.1107/S2052252514026487 PMID: 25866654 Open Access Show Abstract ▼ Abstract: Lipidic cubic phases (LCPs) have emerged as successful matrixes for the crystallization of membrane proteins. Moreover, the viscous LCP also provides a highly effective delivery medium for serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs). Here, the adaptation of this technology to perform serial millisecond crystallography (SMX) at more widely available synchrotron microfocus beamlines is described. Compared with conventional microcrystallography, LCP-SMX eliminates the need for difficult handling of individual crystals and allows for data collection at room temperature. The technology is demonstrated by solving a structure of the light-driven proton-pump bacteriorhodopsin (bR) at a resolution of 2.4 Å. The room-temperature structure of bR is very similar to previous cryogenic structures but shows small yet distinct differences in the retinal ligand and proton-transfer pathway.	Mar 2015

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I03-Macromolecular Crystallography

Megahertz serial crystallography