A multi-reservoir extruder for time-resolved serial protein crystallography and compound screening at X-ray free-electron lasers

Maximilian Wranik (), Michal W. Kepa (), Emma V. Beale, Daniel James, Quentin Bertrand, Tobias Weinert, Antonia Furrer, Hannah Glover, Dardan Gashi, Melissa Carrillo, Yasushi Kondo, Robin T. Stipp, Georgii Khusainov, Karol Nass, Dmitry Ozerov, Claudio Cirelli, Philip J. M. Johnson, Florian Dworkowski, John H. Beale, Scott Stubbs, Thierry Zamofing, Marco Schneider, Kristina Krauskopf, Li Gao, Oliver Thorn-Seshold, Christoph Bostedt, Camila Bacellar, Michel O. Steinmetz, Christopher Milne and Jörg Standfuss
Additional contact information
Maximilian Wranik: Division of Biology and Chemistry, Paul Scherrer Institut, Villigen-PSI
Michal W. Kepa: Division of Biology and Chemistry, Paul Scherrer Institut, Villigen-PSI
Emma V. Beale: Photon Science Division, Paul Scherrer Institut, Villigen-PSI
Daniel James: Division of Biology and Chemistry, Paul Scherrer Institut, Villigen-PSI
Quentin Bertrand: Division of Biology and Chemistry, Paul Scherrer Institut, Villigen-PSI
Tobias Weinert: Division of Biology and Chemistry, Paul Scherrer Institut, Villigen-PSI
Antonia Furrer: Division of Biology and Chemistry, Paul Scherrer Institut, Villigen-PSI
Hannah Glover: Division of Biology and Chemistry, Paul Scherrer Institut, Villigen-PSI
Dardan Gashi: Photon Science Division, Paul Scherrer Institut, Villigen-PSI
Melissa Carrillo: Photon Science Division, Paul Scherrer Institut, Villigen-PSI
Yasushi Kondo: Division of Biology and Chemistry, Paul Scherrer Institut, Villigen-PSI
Robin T. Stipp: Division of Biology and Chemistry, Paul Scherrer Institut, Villigen-PSI
Georgii Khusainov: Division of Biology and Chemistry, Paul Scherrer Institut, Villigen-PSI
Karol Nass: Photon Science Division, Paul Scherrer Institut, Villigen-PSI
Dmitry Ozerov: Theory and Data Division, Paul Scherrer Institut, Villigen-PSI
Claudio Cirelli: Photon Science Division, Paul Scherrer Institut, Villigen-PSI
Philip J. M. Johnson: Photon Science Division, Paul Scherrer Institut, Villigen-PSI
Florian Dworkowski: Photon Science Division, Paul Scherrer Institut, Villigen-PSI
John H. Beale: Photon Science Division, Paul Scherrer Institut, Villigen-PSI
Scott Stubbs: Paul Scherrer Institut, Villigen-PSI
Thierry Zamofing: Paul Scherrer Institut, Villigen-PSI
Marco Schneider: Paul Scherrer Institut, Villigen-PSI
Kristina Krauskopf: Ludwig-Maximilians University of Munich
Li Gao: Ludwig-Maximilians University of Munich
Oliver Thorn-Seshold: Ludwig-Maximilians University of Munich
Christoph Bostedt: Photon Science Division, Paul Scherrer Institut, Villigen-PSI
Camila Bacellar: Photon Science Division, Paul Scherrer Institut, Villigen-PSI
Michel O. Steinmetz: Division of Biology and Chemistry, Paul Scherrer Institut, Villigen-PSI
Christopher Milne: Femtosecond X-ray Experiments Instrument, European XFEL GmbH
Jörg Standfuss: Division of Biology and Chemistry, Paul Scherrer Institut, Villigen-PSI

Nature Communications, 2023, vol. 14, issue 1, 1-12

Abstract: Abstract Serial crystallography at X-ray free-electron lasers (XFELs) permits the determination of radiation-damage free static as well as time-resolved protein structures at room temperature. Efficient sample delivery is a key factor for such experiments. Here, we describe a multi-reservoir, high viscosity extruder as a step towards automation of sample delivery at XFELs. Compared to a standard single extruder, sample exchange time was halved and the workload of users was greatly reduced. In-built temperature control of samples facilitated optimal extrusion and supported sample stability. After commissioning the device with lysozyme crystals, we collected time-resolved data using crystals of a membrane-bound, light-driven sodium pump. Static data were also collected from the soluble protein tubulin that was soaked with a series of small molecule drugs. Using these data, we identify low occupancy (as little as 30%) ligands using a minimal amount of data from a serial crystallography experiment, a result that could be exploited for structure-based drug design.

Date: 2023
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DOI: 10.1038/s41467-023-43523-5

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