TY  - JOUR
AU  - Ekeberg, Tomas
AU  - Assalauova, Dameli
AU  - Bielecki, Johan
AU  - Boll, Rebecca
AU  - Daurer, Benedikt J.
AU  - Eichacker, Lutz A.
AU  - Franken, Linda E.
AU  - Galli, Davide E.
AU  - Gelisio, Luca
AU  - Gumprecht, Lars
AU  - Gunn, Laura H.
AU  - Hajdu, Janos
AU  - Hartmann, Robert
AU  - Hasse, Dirk
AU  - Ignatenko, Alexandr
AU  - Koliyadu, Jayanath
AU  - Kulyk, Olena
AU  - Kurta, Ruslan
AU  - Kuster, Markus
AU  - Lugmayr, Wolfgang
AU  - Lübke, Jannik
AU  - Mancuso, Adrian P.
AU  - Mazza, Tommaso
AU  - Nettelblad, Carl
AU  - Ovcharenko, Yevheniy
AU  - Rivas, Daniel E.
AU  - Rose, Max
AU  - Samanta, Amit K.
AU  - Schmidt, Philipp
AU  - Sobolev, Egor
AU  - Timneanu, Nicusor
AU  - Usenko, Sergey
AU  - Westphal, Daniel
AU  - Wollweber, Tamme
AU  - Worbs, Lena
AU  - Xavier, Paul Lourdu
AU  - Yousef, Hazem
AU  - Ayyer, Kartik
AU  - Chapman, Henry N.
AU  - Sellberg, Jonas A.
AU  - Seuring, Carolin
AU  - Vartanyants, Ivan A.
AU  - Küpper, Jochen
AU  - Meyer, Michael
AU  - Maia, Filipe R. N. C.
TI  - Observation of a single protein by ultrafast X-ray diffraction
JO  - Light
VL  - 13
IS  - 1
SN  - 2047-7538
CY  - London
PB  - Nature Publishing Group
M1  - PUBDB-2024-00530
SP  - 15
PY  - 2024
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:38216563
UR  - <Go to ISI:>//WOS:001142025600001
DO  - DOI:10.1038/s41377-023-01352-7
UR  - https://bib-pubdb1.desy.de/record/602204
ER  -