gated by damage because expected number of photons scattered to a Bragg peak is equivalent to that produced by a shorter pulse with the same intensity.

Despite the great progress in coherent imaging using XFEL sources, the holy grail - atomic resolution of a single (non-crystalline) biomolecule [@Neutze2000] - has not yet been realized. Nevertheless, the potential reward for success has kept this pursuit at the forefront of research in XFEL imaging science. One of the limiting factors is radiation damage. For non-crystalline samples, diffraction from the undamaged structure is not enhanced by periodicity and is mixed indistinguishably with the diffraction of a damaged structure. This is seemingly a major setback for the prospects of developing 3D single particle imaging into a high resolution technique for single molecules. For example, Hau-Riege et al.[@HauRiege2005] found that radiation damage causes large discrepancies with the ideal diffracted intensities, which led them to conclude that pulses must be no more than a few femtoseconds long to avoid severe resolution loss. A more recent study with more detailed scattering models reached a similar conclusion[@Ziaja2012]. However, these studies assessed feasibility with metrics inspired by crystallography whose suitability for single molecule imaging is disputed[@Quiney2011]. Without accounting in 