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Journal Article PUBDB-2024-00530
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Observation of a single protein by ultrafast X-ray diffraction

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2024
Nature Publishing Group London

Light 13(1), 15 () [10.1038/s41377-023-01352-7]
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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.

Classification:
Contributing Institute(s):
  1. CFEL-CMI (FS-CFEL-CMI)
  2. FS-CFEL-1 (Group Leader: Henry Chapman) (CFEL-I)
  3. Computational Nanoscale Imaging (CFEL-CNI)
  4. FS-Photon Science (FS-PS)
  5. Uni Hamburg / Experimentalphysik (UNI/EXP)
  6. beauftragt von UNI (UNI/CUI)
Research Program(s):
  1. 633 - Life Sciences – Building Blocks of Life: Structure and Function (POF4-633) (POF4-633)
  2. DFG project 390715994 - EXC 2056: CUI: Advanced Imaging of Matter (390715994) (390715994)
  3. COMOTION - Controlling the Motion of Complex Molecules and Particles (614507) (614507)
  4. Leibniz Preis - Leibiz Programm 2015: Prof. Dr. Henry N. Chapman (DFG-Leibniz-2015-Chapman) (DFG-Leibniz-2015-Chapman)
Experiment(s):
  1. SPB: Single Particles, clusters & Biomolecules (SASE1)
  2. Experiments at CFEL

Appears in the scientific report 2024
Database coverage:
Medline ; Creative Commons Attribution CC BY 4.0 ; DOAJ ; OpenAccess ; Clarivate Analytics Master Journal List ; Current Contents - Engineering, Computing and Technology ; Current Contents - Physical, Chemical and Earth Sciences ; DOAJ Seal ; IF >= 15 ; JCR ; SCOPUS ; Web of Science Core Collection
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Private Collections > >Extern > >HAS-User > >FS-UNI > UNI/CUI
Private Collections > >Extern > >HAS-User > >FS-UNI > UNI/EXP
Private Collections > >CFEL > >FS-CFEL > CFEL-CNI
Private Collections > >CFEL > >FS-CFEL > CFEL-I
Private Collections > >DESY > >FS > FS-CFEL-CMI
Private Collections > >DESY > >FS > FS-PS
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Observation of a single protein by ultrafast X-ray diffraction
[10.1101/2022.03.09.483477]  GO OpenAccess  Download fulltext Files BibTeX | EndNote: XML, Text | RIS

 Record created 2024-01-30, last modified 2025-07-15
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