Richard Neutze

TL;DR: Computer simulations are used to investigate the structural information that can be recovered from the scattering of intense femtosecond X-ray pulses by single protein molecules and small assemblies and predict that ultrashort, high-intensity X-rays from free-electron lasers that are currently under development will provide a new approach to structural determinations with X- rays.

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: A molecular gating mechanism which appears conserved throughout all plant plasma membrane aquaporins is revealed.

TL;DR: Serial femtosecond crystallography (SFX) is applied using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals of the well-characterized model protein lysozyme, demonstrating the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.

TL;DR: The structure reveals the mechanism of native TbCatB inhibition and demonstrates that new biomolecular information can be obtained by the “diffraction-before-destruction” approach of x-ray free-electron lasers from hundreds of thousands of individual microcrystals.