Nicola Coppola

TL;DR: This work offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage, by using pulses briefer than the timescale of most damage processes.

TL;DR: This work shows that high-quality diffraction data can be obtained with a single X-ray pulse from a non-crystalline biological sample, a single mimivirus particle, which was injected into the pulsed beam of a hard-X-ray free-electron laser, the Linac Coherent Light Source.

TL;DR: Measurements indicate that current X-ray free-electron laser technology should enable structural determination from submicrometre protein crystals with atomic resolution, and the shortest apparent pulse lengths occur at the highest resolution.

TL;DR: The European XFEL as discussed by the authors is a hard X-ray free-electron laser (FEL) based on a highelectron-energy superconducting linear accelerator, which allows for the acceleration of many electron bunches within one radio-frequency pulse of the accelerating voltage and, in turn, for the generation of a large number of hard Xray pulses.

TL;DR: The plasma dynamics of single mesoscopic Xe particles irradiated with intense femtosecond x-ray pulses exceeding 10(16) W/cm2 from the Linac Coherent Light Source free-electron laser are investigated and show that for clusters illuminated with intense x-Ray pulses, highly charged ionization fragments in a narrow distribution are created.