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Instruments / Technical Area	Publication Details	Published	Actions
	A simple goniometer-compatible flow cell for serial synchrotron X-ray crystallography Swagatha Ghosh , Doris Zorić , Peter Dahl , Monika Bjelčić , Jonatan Johannesson , Emil Sandelin , Per Borjesson , Alexander Bjorling , Analia Banacore , Petra Edlund , Oskar Aurelius , Mirko Milas , Jie Nan , Anastasya Shilova , Ana Gonzalez , Uwe Mueller , Gisela Branden , Richard Neutze Journal Of Applied Crystallography 56, 449 - 460 DOI: 10.1107/S1600576723001036 Open Access Show Abstract ▼ Abstract: Serial femtosecond crystallography was initially developed for room-temperature X-ray diffraction studies of macromolecules at X-ray free electron lasers. When combined with tools that initiate biological reactions within microcrystals, time-resolved serial crystallography allows the study of structural changes that occur during an enzyme catalytic reaction. Serial synchrotron X-ray crystallography (SSX), which extends serial crystallography methods to synchrotron radiation sources, is expanding the scientific community using serial diffraction methods. This report presents a simple flow cell that can be used to deliver microcrystals across an X-ray beam during SSX studies. This device consists of an X-ray transparent glass capillary mounted on a goniometer-compatible 3D-printed support and is connected to a syringe pump via lightweight tubing. This flow cell is easily mounted and aligned, and it is disposable so can be rapidly replaced when blocked. This system was demonstrated by collecting SSX data at MAX IV Laboratory from microcrystals of the integral membrane protein cytochrome c oxidase from Thermus thermophilus, from which an X-ray structure was determined to 2.12 Å resolution. This simple SSX platform may help to lower entry barriers for non-expert users of SSX.	Apr 2023
NONE-No attached Diamond beamline	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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