دورية أكاديمية

Observation of a single protein by ultrafast X-ray diffraction

التفاصيل البيبلوغرافية
العنوان: Observation of a single protein by ultrafast X-ray diffraction
المؤلفون: Tomas Ekeberg, Dameli Assalauova, Johan Bielecki, Rebecca Boll, Benedikt J. Daurer, Lutz A. Eichacker, Linda E. Franken, Davide E. Galli, Luca Gelisio, Lars Gumprecht, Laura H. Gunn, Janos Hajdu, Robert Hartmann, Dirk Hasse, Alexandr Ignatenko, Jayanath Koliyadu, Olena Kulyk, Ruslan Kurta, Markus Kuster, Wolfgang Lugmayr, Jannik Lübke, Adrian P. Mancuso, Tommaso Mazza, Carl Nettelblad, Yevheniy Ovcharenko, Daniel E. Rivas, Max Rose, Amit K. Samanta, Philipp Schmidt, Egor Sobolev, Nicusor Timneanu, Sergey Usenko, Daniel Westphal, Tamme Wollweber, Lena Worbs, Paul Lourdu Xavier, Hazem Yousef, Kartik Ayyer, Henry N. Chapman, Jonas A. Sellberg, Carolin Seuring, Ivan A. Vartanyants, Jochen Küpper, Michael Meyer, Filipe R. N. C. Maia
المصدر: Light: Science & Applications, Vol 13, Iss 1, Pp 1-11 (2024)
بيانات النشر: Nature Publishing Group, 2024.
سنة النشر: 2024
المجموعة: LCC:Applied optics. Photonics
LCC:Optics. Light
مصطلحات موضوعية: Applied optics. Photonics, TA1501-1820, Optics. Light, QC350-467
الوصف: 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 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.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 2047-7538
العلاقة: https://doaj.org/toc/2047-7538Test
DOI: 10.1038/s41377-023-01352-7
الوصول الحر: https://doaj.org/article/990d0d21eb0d4351888a9b904a55ebd1Test
رقم الانضمام: edsdoj.990d0d21eb0d4351888a9b904a55ebd1
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:20477538
DOI:10.1038/s41377-023-01352-7