Speaker
Description
Ultra-short, ultra-bright X-ray pulses from Free Electron Lasers are a viable tool for observing diffraction from two-dimensional (2D) crystals, unlike synchrotron-based data collection, extending the possibilities of structural determinations in membrane proteins.
Using serial diffraction frames from bacteriorhodopsin 2D crystals we extended the resolution limit of zero-tilt data to 4 A (detector-limited) by summing equivalent portions of images, and developed a method to reconstruct diffraction intensities along Bragg lines, from which structural information can be gained.
Using these methods a data collection strategy (100'000 - 200'000 images at high tilt angles) allowing to detect structural changes in the length-scale of a few A in a pump-probe configuration can be envisaged.
