Oral Presentation The 43rd Lorne Conference on Protein Structure and Function 2018

Time-resolved serial femtosecond crystallography studies at an X-ray free electron laser reveals structural changes in bacteriorhodopsin (#14)

Richard Neutze 1 , Eriko Nango 2 , Antoine Royant 3 , Jörg Standfuss 4 , Cecilia Wickstrand 1
  1. University of Gothenburg, Sweden
  2. Kyoto University & Riken SPring-8 Center (SACLA), Japan
  3. ESRF, France
  4. Przemyslaw Nogly, Paul Scherer Institute, Switzerland

X-ray free electron lasers (XFEL) provide a billion-fold jump in the peak X-ray brilliance when compared with synchrotron radiation. One area where XFEL radiation is having an impact is time-resolved structural studies of protein conformational changes. I will describe how we used time resolved serial femtosecond crystallography at an XFEL to probe light-driven structural changes in bacteriorhodopsin. Bacteriorhodopsin is a light-driven proton pump which has long been used as a model system in biophysics. The mechanism by which light-driven isomerization of a retinal chromophore is coupled to the transport of protons “up-hill” against a transmembrane proton concentration gradient involves protein structural changes. Collaborative studies performed at SACLA (An XFEL in Japan) have probed structural changes in microcrystals on a time-scale from nanoseconds to milliseconds. Structural results from these studies enabled a complete picture of structural changes occurring during proton pumping by bacteriorhodopsin to be recovered (Nango et al., 2016).

  1. Nango, E., et al. A three-dimensional movie of structural changes in bacteriorhodopsin. Science 354, 1552-1557 (2016).