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@ARTICLE{Ekeberg:599083,
author = {Ekeberg, Tomas and Assalauova, Dameli and Bielecki, Johan
and Boll, Rebecca and Daurer, Benedikt J. and Eichacker,
Lutz A. and Franken, Linda E. and Galli, Davide E. and
Gelisio, Luca and Gumprecht, Lars and Gunn, Laura H. and
Hajdu, Janos and Hartmann, Robert and Hasse, Dirk and
Ignatenko, Alexandr and Koliyadu, Jayanath and Kulyk, Olena
and Kurta, Ruslan and Kuster, Markus and Lugmayr, Wolfgang
and Lübke, Jannik and Mancuso, Adrian P. and Mazza, Tommaso
and Nettelblad, Carl and Ovcharenko, Yevheniy and Rivas,
Daniel E. and Samanta, Amit K. and Schmidt, Philipp and
Sobolev, Egor and Timneanu, Nicusor and Usenko, Sergej and
Westphal, Daniel and Wollweber, Tamme and Worbs, Lena and
Xavier, P. Lourdu and Yousef, Hazem and Ayyer, Kartik and
Chapman, Henry N. and Sellberg, Jonas A. and Seuring,
Carolin and Vartanyants, Ivan A. and Küpper, Jochen and
Meyer, Michael and Maia, Filipe R. N. C.},
title = {{O}bservation of a single protein by ultrafast {X}-ray
diffraction},
reportid = {PUBDB-2023-07149},
year = {2023},
note = {The paper is accepted for publication in Light: Science
$\&$ Applications but not published yet. Information from
Amit Samanta.},
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.},
cin = {FS-CFEL-CMI / FS-CFEL-1 / UNI/CUI / UNI/EXP / FS-PS},
cid = {I:(DE-H253)FS-CFEL-CMI-20220405 /
I:(DE-H253)FS-CFEL-1-20120731 /
$I:(DE-H253)UNI_CUI-20121230$ /
$I:(DE-H253)UNI_EXP-20120731$ / I:(DE-H253)FS-PS-20131107},
pnm = {633 - Life Sciences – Building Blocks of Life: Structure
and Function (POF4-633) / DFG project 390715994 - EXC 2056:
CUI: Advanced Imaging of Matter (390715994) / COMOTION -
Controlling the Motion of Complex Molecules and Particles
(614507) / Leibniz Preis - Leibiz Programm 2015: Prof. Dr.
Henry N. Chapman (DFG-Leibniz-2015-Chapman) / DFG project
194651731 - EXC 1074: Hamburger Zentrum für ultraschnelle
Beobachtung (CUI): Struktur, Dynamik und Kontrolle von
Materie auf atomarer Skala (194651731)},
pid = {G:(DE-HGF)POF4-633 / G:(GEPRIS)390715994 /
G:(EU-Grant)614507 / G:(DE-H253)DFG-Leibniz-2015-Chapman /
G:(GEPRIS)194651731},
experiment = {EXP:(DE-H253)XFEL-Exp-20150101 /
EXP:(DE-H253)CFEL-Exp-20150101},
typ = {PUB:(DE-HGF)25},
doi = {10.1101/2022.03.09.483477},
url = {https://bib-pubdb1.desy.de/record/599083},
}