Observation of a single protein by ultrafast X-ray diffraction

DOI: 10.1038/s41377-023-01352-7

Authors: Tomas Ekeberg (Uppsala University) , Dameli Assalauova (Deutsches Electronen-Synchrotron DESY) , Johan Bielecki (European XFEL) , Rebecca Boll (European XFEL) , Benedikt J. Daurer (Diamond Light Source) , Lutz A. Eichacker (University of Stavanger) , Linda E. Franken (Leibniz Institute for Experimental Virology (HPI) , Davide E. Galli (Università degli Studi di Milano) , Luca Gelisio (Deutsches Electronen-Synchrotron DESY) , Lars Gumprecht (Center for Free-Electron Laser Science, DESY) , Laura H. Gunn (Uppsala University; Cornell University) , Janos Hajdu (Uppsala University) , Robert Hartmann (PNSensor GmbH) , Dirk Hasse (Uppsala University) , Alexandr Ignatenko (Deutsches Electronen-Synchrotron DESY) , Jayanath Koliyadu (European XFEL; KTH Royal Institute of Technology) , Olena Kulyk (ELI Beamlines/IoP Institute of Physics AS CR) , Ruslan Kurta (European XFEL) , Markus Kuster (European XFEL) , Wolfgang Lugmayr (Centre for Structural Systems Biology (Germany); University Medical Center Hamburg-Eppendorf (UKE)) , Jannik Lübke (Center for Free-Electron Laser Science, DESY; Universität Hamburg) , Adrian P. Mancuso (European XFEL; La Trobe University) , Tommaso Mazza (European XFEL) , Carl Nettelblad (Uppsala University) , Yevheniy Ovcharenko (European XFEL) , Daniel E. Rivas (European XFEL) , Max Rose (Deutsches Electronen-Synchrotron DESY) , Amit K. Samanta (Center for Free-Electron Laser Science, DESY) , Philipp Schmidt (European XFEL) , Egor Sobolev (European XFEL; European Molecular Biology Laboratory) , Nicusor Timneanu (Uppsala University) , Sergey Usenko (European XFEL) , Daniel Westphal (Uppsala University) , Tamme Wollweber (Universität Hamburg; Max Planck Institute for the Structure and Dynamics of Matter; Center for Free-Electron Laser Science) , Lena Worbs (Center for Free-Electron Laser Science, DESY; Universität Hamburg) , Paul Lourdu Xavier (European XFEL; Center for Free-Electron Laser Science, DESY; Max Planck Institute for the Structure and Dynamics of Matter) , Hazem Yousef (European XFEL) , Kartik Ayyer (Universität Hamburg; Max Planck Institute for the Structure and Dynamics of Matter; Center for Free-Electron Laser Science) , Henry N. Chapman (Center for Free-Electron Laser Science, DESY; Universität Hamburg) , Jonas A. Sellberg (KTH Royal Institute of Technology) , Carolin Seuring (Centre for Structural Systems Biology (Germany); Universität Hamburg) , Ivan A. Vartanyants (Deutsches Electronen-Synchrotron DESY) , Jochen Küpper (Center for Free-Electron Laser Science, DESY; Universität Hamburg) , Michael Meyer (European XFEL) , Filipe R. N. C. Maia (Uppsala University; Lawrence Berkeley National Laboratory)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Light: Science & Applications , VOL 13

State: Published (Approved)
Published: January 2024

Abstract: The idea of using ultrashort X-ray pulses to obtain images of single proteins frozen in time has fascinated and inspired many. It was one of the arguments for building X-ray free-electron lasers. According to theory, the extremely intense pulses provide sufficient signal to dispense with using crystals as an amplifier, and the ultrashort pulse duration permits capturing the diffraction data before the sample inevitably explodes. This was first demonstrated on biological samples a decade ago on the giant mimivirus. Since then, a large collaboration has been pushing the limit of the smallest sample that can be imaged. The ability to capture snapshots on the timescale of atomic vibrations, while keeping the sample at room temperature, may allow probing the entire conformational phase space of macromolecules. Here we show the first observation of an X-ray diffraction pattern from a single protein, that of Escherichia coli GroEL which at 14 nm in diameter is the smallest biological sample ever imaged by X-rays, and demonstrate that the concept of diffraction before destruction extends to single proteins. From the pattern, it is possible to determine the approximate orientation of the protein. Our experiment demonstrates the feasibility of ultrafast imaging of single proteins, opening the way to single-molecule time-resolved studies on the femtosecond timescale.

Subject Areas: Technique Development, Biology and Bio-materials

Facility: European XFEL

Added On: 15/01/2024 09:32

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Technique Development - Life Sciences & Biotech Structural biology Life Sciences & Biotech

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