بيانات النشر: Uppsala universitet, Molekylär biofysik
Uppsala universitet, Avdelningen för beräkningsvetenskap
Uppsala universitet, Tillämpad beräkningsvetenskap
Uppsala universitet, Science for Life Laboratory, SciLifeLab
Uppsala universitet, Kemisk och biomolekylär fysik
European XFEL, Holzkoppel 4, 22869, Schenefeld, Germany
Diamond Light Source, Harwell Science & Innovation Campus, Didcot, OX11 0DE, UK
Plant Biology Section, School of Integrative Plant Science, Cornell University, Ithaca, NY, 14853, USA
NERSC, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA
نبذة مختصرة : 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.
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