Speaker
Description
The quest to image single molecules played a crucial role in the development of X-ray free-electron lasers (XFELs). The ultra-bright, ultrafast pulses of XFELs enable the recording of a particle’s diffraction pattern before radiation damage destroys it—a concept first proposed by Neutze et al. (Nature, 2000) and experimentally demonstrated at FLASH over a decade ago (Chapman et al., Nature Physics, 2006). Since then, flash X-ray imaging (FXI) has been successfully applied to imaging live cells (van der Schot et al., Nature Communications, 2015), cellular organelles (Hantke et al., Nature Photonics, 2014), and viruses in both two (Seibert et al., Nature, 2011) and three dimensions (Ekeberg et al., PRL, 2015).
The advent of the European XFEL ushered in an era of high-intensity, high-repetition-rate, and high-data-rate XFELs, demonstrating that FXI could fully leverage these advancements. However, the ultimate goal of achieving sub-nanometer, high-resolution imaging remains unfulfilled.
In this talk, I will present the first three-dimensional X-ray image of single proteins in the gas phase. Additionally, I will discuss microsecond time-resolved measurements of protein dynamics in solution, obtained via SAXS/WAXS at the European XFEL. Finally, I will share preliminary results on pushing X-ray solution scattering to the limit of one particle per shot, FXI in solution, highlighting how ultrathin liquid sheets, coupled with advancements in X-ray optics, hold promise for ultrafast, nanoscale imaging of biological macromolecules in solution at room temperature.
| Scientific Topics | Imaging |
|---|