Uwe Weierstall

TL;DR: For a typical protein molecule (lysozyme) with anisotropic polarizability, it is found that up to 1 kW of continuous-wave near-infrared laser power may be needed to produce sufficiently accurate alignment for direct observation of the secondary structure of proteins in the reconstructed potential or charge-density map.

TL;DR: The first powder diffraction patterns from a membrane protein, photosystem I, with crystallite sizes of less than 500 nm are presented, and these preliminary patterns show the lowest-order reflections, which agree quantitatively with theoretical calculations of the powder profile.

TL;DR: The rhodopsin-arrestin crystal structure solved with SFX represents the first near-atomic resolution structure of a GPCR-Arrestin complex, provides structural insights into understanding of arrestin-mediated GPCRs signaling, and demonstrates the great potential of this SFX-XFEL technology for accelerating crystal structure determination of challenging proteins and protein complexes.

TL;DR: In this paper, the authors used femtosecond X-ray free electron laser (XFEL) pulses to obtain structural measurements from crystals so small that diffusion of a ligand can be timed to initiate a reaction before diffraction.

TL;DR: It is found that multiple single-file protein beams will be needed for sub-nanometer resolution on current third-generation synchrotrons, but not on fourth-generation designs, where reconstruction of secondary protein structure at a resolution of 7 A should be possible with relatively short exposures.