GDR XFEL
Science with XFEL

Biologie structurale – Publications

  1. Barends TRM., et al., Influence of pump laser fluence on ultrafast myoglobin structural dynamics. Nature 626, 905 (2024)
  2. Maestre-Reyna M., et al., Visualizing the DNA repair process by a photolyase at atomic resolution. Science 382, eadd7795 (2023)
  3. Hadjidemetriou K., et al., Time-resolved serial femtosecond crystallography on fatty-acid photode­carboxylase: lessons learned. Acta Cryst D 78, 1131 (2022).
  4. Adam V., et al., Rational Control of Off-State Heterogeneity in a Photoswitchable Fluorescent Protein Provides Switching Contrast Enhancement. Chem. Phys. Chem. e202200192 (2022).
  5. Tetreau G. et al., De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals Nature Communications 13, 4376 (2022).
  6. De Zitter E. et al., Xtrapol8 enables automatic elucidation of low-occupancy intermediate-states in crystallographic studies. Communication Biology 5, 640 (2022).
  7. Sorigué D., et al., Mechanism and dynamics of fatty acid photodecarboxylase. Science 372, eabd5687 (2021).
  8. Gorel A., et al., Shock Damage Analysis in Serial Femtosecond Crystallography Data Collected at MHz X-ray Free-Electron Lasers. Crystals 10, 1145 (2021).
  9. Tetreau G. et al., Serial femtosecond crystallography on in vivo-grown crystals drives elucidation of mosquitocidal Cyt1Aa bioactivation cascade. Nature Communication 11, 1153 (2020).
  10. de la Mora E., et al. Radiation damage and dose limits in serial synchrotron crystallography at cryo- and room temperatures. Proc. Natl. Acad. Sci. USA 117, 4142 (2020).
  11. Woodhouse J., et al. Photoswitching mechanism of a fluorescent protein revealed by time-resolved crystallography and transient absorption spectroscopy. Nature communications 11, 741 (2020).
  12. Grünbein M. L., et al., MHz data collection of a microcrystalline mixture of different jack bean proteins.  Sci Data 6, 18 (2019).
  13. Heyes D. J., et al. Light-induced structural changes in a full-length cyanobacterial phytochrome probed by time-resolved X-ray scattering. Comms. Biol. 2, 1 (2019).
  14. Dwayne Miller R. J., et al. Three-dimensional view of ultrafast dynamics in photoexcited bacteriorhodopsin. Nature communications 10, 3177 (2019).
  15. Coquelle N., et al. Chromophore twisting in the excited state of a photoswitchable fluorescent protein captured by time-resolved serial femtosecond crystallography. Nature Chemistry 10, 31 (2018).
  16. Grünbein M. L., et al. Megahertz data collection from protein microcrystals at an X-ray free-electron laser. Nature Communications 9, 3487 (2018).
  17. Schiro G., et al. Simple and expeditious system for photo-converting light-sensitive proteins in serial crystallography experiments. J Appl. Cryst. 50, 932 (2017).
  18. Colletier J.P., et al. Serial femtosecond crystallography and ultrafast absorption spectroscopy of the photoswitchable fluorescent protein IrisFP. J. Phys. Chem. Lett. 7, 882 (2016).
  19. Colletier J.P., et al. De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure. Nature 539, 43 (2016).
  20. Coquelle N., et al. Raster-scanning serial protein crystallography using micro- and nano-focused synchrotron beams. Acta Crystallogr D Biol Crystallogr 71, 1184 (2015).
  21. Levantino M., et al. Observing heme doming in myoglobin with femtosecond X-ray absorption spectroscopy. Structural Dynamics 2, 041713 (2015).
  22. Levantino M., et al. Ultrafast myoglobin structural dynamics observed with an X-ray free-electron laser. Nature Communications 6, 6772  (2015).
  23. Soragni A., et al. Toxicity of eosinophil MBP is repressed by intracellular crystallization and promoted by extracellular aggregation. Mol. Cell 57, 1011 (2015).
  24. Gebhardt R., et al. Virus particle assembly into crystalline domains enabled by the coffee ring effect. Soft Matter 10, 5458 (2014).
  25. Sawaya M. R., et al. Protein crystal structure obtained at 2.9 Å resolution from injecting bacterial cells into an X-ray free-electron laser beam. Proc. Natl. Acad. Sci. USA 111, 12769 (2014).