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Observation of a single protein by ultrafast X-ray diffraction
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
European XFEL, Holzkoppel 4, 22869, Schenefeld, Germany.ORCID iD: 0000-0002-3012-603X
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2024 (English)In: Light: Science & Applications, ISSN 2095-5545, E-ISSN 2047-7538, Vol. 13, no 1, article id 15Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
Springer Nature, 2024. Vol. 13, no 1, article id 15
National Category
Biophysics
Identifiers
URN: urn:nbn:se:uu:diva-520488DOI: 10.1038/s41377-023-01352-7ISI: 001142025600001PubMedID: 38216563OAI: oai:DiVA.org:uu-520488DiVA, id: diva2:1827159
Funder
German Research Foundation (DFG), 152/772-1German Research Foundation (DFG), 152/774-1German Research Foundation (DFG), 152/775-1German Research Foundation (DFG), 152/776-1German Research Foundation (DFG), 152/777-1German Research Foundation (DFG), 390715994EU, European Research Council, 614507European Regional Development Fund (ERDF), CZ.02.1.01/0.0/0.0/15_003/0000447Swedish Research Council, 2017-05336Swedish Research Council, 2018-00234Swedish Research Council, 2019-03935Swedish Foundation for Strategic Research, ITM17-0455Available from: 2024-01-12 Created: 2024-01-12 Last updated: 2024-01-30Bibliographically approved

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Ekeberg, TomasBielecki, JohanDaurer, Benedikt J.Gunn, Laura H.Hajdu, JanosHasse, DirkNettelblad, CarlTimneanu, NicusorWestphal, DanielMaia, Filipe R. N. C.

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Ekeberg, TomasBielecki, JohanDaurer, Benedikt J.Gunn, Laura H.Hajdu, JanosHasse, DirkNettelblad, CarlTimneanu, NicusorWestphal, DanielMaia, Filipe R. N. C.
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Molecular biophysicsDivision of Scientific ComputingComputational ScienceScience for Life Laboratory, SciLifeLabChemical and Bio-Molecular Physics
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