The European XFEL (EuXFEL) enables high resolution and time-resolved structural studies of biological systems. Diffraction, scattering and spectroscopy experiments with a MHz pulse repetition rate, in combination with optical pump-probe or mixing set-ups, give new insights into protein motion and dynamics. To accommodate the MHz repetition rate, sample delivery methods are in demand which...
X-ray emission spectroscopy (XES) complements structural techniques like serial femtosecond crystallography (SFX) by providing insights into the electronic states at specific sites within a sample. At X-ray free-electron lasers, simultaneous SFX and XES measurements using a single pulse have already been performed — such as the determination of the oxidation states in metalloproteins. By using...
TRISS (TRapped Ion Spectrometer Setup) is a novel experimental station at the MAX IV synchrotron facility, designed to investigate fundamental molecular processes relevant to biomolecular and biochemical physics. TRISS uses an electrospray ionization (ESI) source to create ions, which are then fragmented using photons, electrons, or gas. The TRISS setup combines a segmented linear ion trap...
Diffractive single-particle imaging (SPI) using X-ray free-electron
lasers (XFELs) offers a promising approach for determining protein
structures without crystallization (Neutze2000) . For successful
reconstruction thousands of diffraction images of individual proteins
have to be assembled. It has been shown with molecular dynamics
simulations that proteins carrying a dipole moment can be...
Serial macromolecular crystallography (SMX) has emerged as a transformative technique enabling measurements across expansive parameter spaces in structural biology. Here I will talk about the evolution of serial crystallography techniques, particularly focusing on developments for time-resolved, pH-responsive, and temperature-controlled experiments and their application in unraveling dynamic...
