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Femtosecond x-ray nanocrystallography exploiting XFEL radiation is anemerging method for protein structure determination using crystals with sizesranging from a few tens to a few hundreds nanometers. Crystals are randomly hitby XFEL pulses, producing diffraction patterns at unknown orientations. One candetermine these orientations by studying the diffraction patterns themselves,i.e. by indexing the Bragg peaks. The number of indexed individual images andthe SASE bandwidth are inherently linked, because increasing the number ofBragg peaks per individual image requires increasing the bandwidth of thespectrum. This calls for a few percent SASE bandwidth, resulting in an increasein the number of indexed images at the same number of hits. Based onstart-to-end simulations for the baseline of the European XFEL, we demonstratehere that it is possible to achieve up to a tenfold increase in SASE bandwidth,compared with the nominal mode of operation. This provides a route for furtherincreasing the efficiency of protein structure determination at the EuropeanXFEL. We illustrate this concept with simulations of lysozyme nanocrystals.

Extension of SASE bandwidth up to 2% as a way to increase the efficiency  of protein structure determination by x-ray nanocrystallography at the  European XFEL