Speaker
Description
X-ray free electron lasers (XFEL) have facilitated the development of time-resolved serial femtosecond crystallography (TR-SFX) approaches to study protein structural changes [1]. This method relies upon the continuous replacement of microcrystals using micro-jet (or other) technologies and has many advantages relative to traditional time-resolved Laue diffraction methods using synchrotron radiation [2]. Photosynthetic reaction centres are integral membrane proteins which harvest the energy content of sunlight in order to power the movement of electrons. We collected TR-SFX data at the LCLS in order to observe light induced structural changes in a bacterial photosynthetic reaction centre. Our observations revealed how the light-induced movement of electrons induced a complementary structural response of the protein which stabilized the charge-separated state [3].
[1] Tenboer, J., et al. Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein. Science 346,1242-1246 (2014).
[2] A. Wöhri et al., Light-induced structural changes in a photosynthetic reaction center caught by Laue diffraction, Science 328, 630-633 (2010).
[3] R. Dods et al., Ultrafast structural changes within a photosynthetic reaction centre, Nature 589, 310-314 (2021)
