Observation of a single protein by ultrafast X-ray diffraction
Author:
Ekeberg Tomas, Assalauova Dameli, Bielecki Johan, Boll Rebecca, Daurer Benedikt J., Eichacker Lutz A., Franken Linda E., Galli Davide E., Gelisio Luca, Gumprecht Lars, Gunn Laura H., Hajdu Janos, Hartmann Robert, Hasse Dirk, Ignatenko Alexandr, Koliyadu Jayanath, Kulyk Olena, Kurta Ruslan, Kuster Markus, Lugmayr Wolfgang, Lübke Jannik, Mancuso Adrian P., Mazza Tommaso, Nettelblad Carl, Ovcharenko Yevheniy, Rivas Daniel E., Samanta Amit K., Schmidt Philipp, Sobolev Egor, Timneanu Nicusor, Usenko Sergej, Westphal Daniel, Wollweber Tamme, Worbs Lena, Xavier P. Lourdu, Yousef Hazem, Ayyer KartikORCID, Chapman Henry N., Sellberg Jonas A., Seuring Carolin, Vartanyants Ivan A., Küpper Jochen, Meyer Michael, Maia Filipe R.N.C.
Abstract
AbstractThe 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 collaboration4has 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 ofEscherichia coliGroEL which at 14 nm in diameter7is 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.
Publisher
Cold Spring Harbor Laboratory
Cited by
5 articles.
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