AVS 65th International Symposium & Exhibition
    Novel Trends in Synchrotron and FEL-Based Analysis Focus Topic Thursday Sessions
       Session SA-ThP

Paper SA-ThP4
A New Route for the Determination of Protein Structure in Physiological Environment through Coherent Diffraction Imaging.

Thursday, October 25, 2018, 6:00 pm, Room Hall B

Session: Novel Trends in Synchrotron and FEL-Based Analysis Focus Topic Poster Session
Presenter: Danny Fainozzi, university of Trieste / Elettra Synchrotron, Italy
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Revealing the structure of complex biological macromolecules, such as proteins, is an essential step for understanding the chemical mechanisms that determine the diversity of their functions. Synchrotron based x-ray crystallography and cryo-electron microscopy have made major contributions in determining thousands of protein structures even from micro-sized crystals. They suffer from some limitations that have not been overcome, such as radiation damage, the natural inability to crystallize of a number of proteins and experimental conditions for structure determination that are incompatible with the physiological environment. Today the ultrashort and ultra-bright pulses of X-ray free-electron lasers (XFELs) have made attainable the dream to determine protein structure before radiation damage starts to destroy the samples. However, the signal-to-noise ratio remains a great challenge to obtain usable diffraction patterns from a single protein molecule. We describe here a new methodology that should overcome the signal and protein crystallization limits. Using a multidisciplinary approach, we propose to create a two dimensional protein array with defined orientation attached on a self-assembled-monolayer . We develop a literature-based, flexible toolbox capable of assembling different proteins on a functionalized surface while keeping them under physiological conditions during the experiment, using a water-confining graphene cover.