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Visualization of protein motions using temperature-jump crystallography

An infrared laser-induced temperature jump provides a rapid and broadly applicable perturbation to protein dynamics. Temperature-jump crystallography was paired with time-resolved X-ray crystallography to study the dynamic enzyme lysozyme. Measurements with and without a functional inhibitor revealed different patterns in the propagation of motion throughout the enzyme.

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Fig. 1: Lysozyme dynamics induced by a temperature jump.


  1. van den Bedem, H. & Fraser, J. S. Integrative, dynamic structural biology at atomic resolution—it’s about time. Nat. Methods 12, 307–318 (2015). A review outlining a broad variety of approaches to studying protein dynamics.

    Article  PubMed  PubMed Central  Google Scholar 

  2. Schmidt, M. Time-resolved macromolecular crystallography at modern X-ray sources. Methods Mol. Biol. 1607, 273–294 (2017). A review highlighting challenges and developments in methods for time-resolved crystallography.

    Article  CAS  PubMed  Google Scholar 

  3. Gruebele, M., Sabelko, J., Ballew, R. & Ervin, J. Laser temperature jump induced protein refolding. Acc. Chem. Res. 31, 699–707 (1998). A review covering infrared-induced temperature jumps coupled with spectroscopy to study proteins.

    Article  CAS  Google Scholar 

  4. Keedy, D. A. et al. Mapping the conformational landscape of a dynamic enzyme by multitemperature and XFEL crystallography. eLife 4, e07574 (2015). This paper reveals the effects of temperature on protein structures at thermal equilibrium.

    Article  PubMed  PubMed Central  Google Scholar 

  5. Thompson, M. C. et al. Temperature-jump solution X-ray scattering reveals distinct motions in a dynamic enzyme. Nat. Chem. 11, 1058–1066 (2019). This paper reports the use of temperature-jump paired with solution X-ray scattering to gain insight into functional protein dynamics.

    Article  CAS  PubMed  PubMed Central  Google Scholar 

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This is a summary of: Wolff, A. M. et al. Mapping protein dynamics at high spatial resolution with temperature-jump X-ray crystallography. Nat. Chem. (2023).

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Visualization of protein motions using temperature-jump crystallography. Nat. Chem. 15, 1497–1498 (2023).

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