Watching proteins function with time-resolved x-ray crystallography
Open accessAbstract
Macromolecular crystallography was immensely successful in the last two decades. To a large degree this success resulted from use of powerful third generation synchrotron x-ray sources. An expansive database of more than 100 000 protein structures, of which many were determined at resolution better than 2 Å, is available today. With this achievement, the spotlight in structural biology is shifting from determination of static structures to elucidating dynamic aspects of protein function. A powerful tool for addressing these aspects is time-resolved crystallography, where a genuine biological function is triggered in the crystal with a goal of capturing molecules in action and determining protein kinetics and structures of intermediates (Schmidt et al 2005a Methods Mol. Biol . 305 115–54, Schmidt 2008 Ultrashort Laser Pulses in Biology and Medicine (Berlin: Springer) pp 201–41, Neutze and Moffat 2012 Curr. Opin. Struct. Biol . 22 651–9, Šrajer 2014 The Future of Dynamic Structural Science (Berlin: Springer) pp 237–51). In this approach, short and intense x-ray pulses are used to probe intermediates in real time and at room temperature, in an ongoing reaction that is initiated synchronously and rapidly in the crystal. Time-resolved macromolecular crystallography with 100 ps time resolution at synchrotron x-ray sources is in its mature phase today, particularly for studies of reversible, light-initiated reactions. The advent of the new free electron lasers for hard x-rays (XFELs; 5–20 keV), which provide exceptionally intense, femtosecond x-ray pulses, marks a new frontier for time-resolved crystallography. The exploration of ultra-fast events becomes possible in high-resolution structural detail, on sub-picosecond time scales (Tenboer et al 2014 Science 346 1242–6, Barends et al 2015 Science 350 445–50, Pande et al 2016 Science 352 725–9). We review here state-of-the-art time-resolved crystallographic experiments both at synchrotrons and XFELs. We also outline challenges and further developments necessary to broaden the application of these methods to many important proteins and enzymes of biomedical relevance.
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Developments in experimental techniques such as ultrafast spectroscopy, single molecule spectroscopy, time-resolved microscopy and single particle imaging have enabled study of biological dynamics on increasingly small length and time scales, revealing processes necessary for living function that depend on a delicate interplay between quantum and classical physical effects.
“Recently, developments in experimental techniques such as ultrafast spectroscopy [6], single molecule spectroscopy [7 -11], timeresolved microscopy [12 -14] and single particle imaging [15 -18] have enabled us to study biological dynamics on increasingly small length and time scales, revealing a variety of processes necessary for the function of the living system that depend on a delicate interpl”
From The future of quantum biology (2018) · cites this paper as [12]
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- Authors
- Šrajer, V., & Schmidt, M.
- Affiliations
- University of Chicago (US)
- University of Wisconsin–Milwaukee (US)
- Venue
- Journal of Physics D: Applied Physics
- Publisher
- IOP Publishing
- Published
- 2017-08-22
- Volume
- 50
- Issue
- 37
- Pages
- 373001
- ISSN
- 0022-3727 (ISSN-L)
- 1361-6463
- PMC
- PMC5771432
- OpenAlex
- W2724538250
- Cited by
- 67
- References
- 141
- Citations by year
- 2026: 2 · 2025: 6 · 2024: 7 · 2023: 9 · 2022: 10 · 2021: 7 · 2020: 15 · 2019: 7 · 2018: 4
- FWCI
- 3.00
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- Journal of Physics D Applied Physics (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of General Medical Sciences (R24GM111072)
- National Science Foundation (NFS-1231306)
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Physical Sciences › Physics and Astronomy › Radiation › Advanced X-ray Imaging Techniques
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- protein dynamics, protein intermediates, free-electron laser, synchrotron X-ray sources, femtosecond X-ray pulses, protein kinetics, enzyme mechanism, ultrafast structural dynamics
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