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  Observation of a single protein by ultrafast X-ray diffraction

Ekeberg, T., Assalauova, D., Bielecki, J., Boll, R., Daurer, B. J., Eichacker, L. A., et al. (2022). Observation of a single protein by ultrafast X-ray diffraction. doi:10.1101/2022.03.09.483477.

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2022.03.09.483477v1.full.pdf (Preprint), 2MB
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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity.

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 Creators:
Ekeberg, T.1, Author
Assalauova, D.1, Author
Bielecki, J.1, Author
Boll, R.1, Author
Daurer, B. J.1, Author
Eichacker, L. A.1, Author
Franken, L. E.1, Author
Galli, D. E.1, Author
Gelisio, L.1, Author
Gumprecht, L.1, Author
Gunn, L. H.1, Author
Hajdu, J.1, Author
Hartmann, R.1, Author
Hasse, D.1, Author
Ignatenko, A.1, Author
Koliyadu, J.1, Author
Kulyk, O.1, Author
Kurta, R.1, Author
Kuster, M.1, Author
Lugmayr, W.1, Author
Lübke, J.1, AuthorMancuso, A. P.1, AuthorMazza, T.1, AuthorNettelblad, C.1, AuthorOvcharenko, Y.1, AuthorRivas, D. E.1, AuthorRose, M.1, AuthorSamanta, A. K.1, AuthorSchmidt, P.1, AuthorSobolev, E.1, AuthorTimneanu, N.1, AuthorUsenko, S.1, AuthorWestphal, D.1, AuthorWollweber, T.2, 3, 4, 5, Author              Worbs, L.1, AuthorXavier, P. L.1, AuthorYousef, H.1, AuthorAyyer, K.2, 4, 5, Author              Chapman, H. N.1, AuthorSellberg, J. A.1, AuthorSeuring, C.1, AuthorVartanyants, I. A.1, AuthorKüpper, J.1, AuthorMeyer, M.1, AuthorMaia, F. R.N.C.1, Author more..
Affiliations:
1external, ou_persistent22              
2The Hamburg Center for Ultrafast Imaging, Universität Hamburg, ou_persistent22              
3Department of Physics, Universität Hamburg, ou_persistent22              
4Computational Nanoscale Imaging, Condensed Matter Dynamics Department, Max Planck Institute for the Structure and Dynamics of Matter, Max Planck Society, ou_3012829              
5Center for Free-Electron Laser Science, Hamburg, ou_persistent22              

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 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 theory1, 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 explodes2. This was first demonstrated on biological samples a decade ago on the giant mimivirus3. Since then a large collaboration4 has been pushing the limit of the smallest sample that can be imaged5,6. 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 diameter7 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.

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Language(s): eng - English
 Dates: 2022-03-12
 Publication Status: Published online
 Pages: 20
 Publishing info: -
 Table of Contents: -
 Rev. Type: No review
 Identifiers: DOI: 10.1101/2022.03.09.483477
 Degree: -

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