Neutron crystallography and sub-atomic X-ray crystallography complement each other in defining hydrogen positions in macromolecules. Significant advances have been made but much effort is still required if neutron crystallography is to become a mainstream activity.

Using synchrotron radiation, diffraction data extending to 0.70 Å resolution were collected from crystals of the small protein crambin at room temperature (297 K), and the structure was refined with spherical-atom approximation to an R factor of 0.0591, revealing (i) protein regions with multiple conformations, (ii) extended water networks correlated with protein conformations and (iii) minimal radiation damage. The structure sets a standard for room-temperature refinement of macromolecular targets and provides accurate data for modeling protein–solvent interactions.

This article demonstrates how a nano-focused electron beam can be used to collect sparse diffraction patterns from ∼40 nm regions of a macromolecular crystal that are subsequently digitally recombined into a tilt series suitable for ab initio phasing. By synthesizing signals from specific sub-regions of a crystal after data are collected, the findings provide the basis for capturing atomic level information from mosaic or partially ordered crystals that might otherwise be overlooked.

Active human β-glucocerebrosidase was produced in baculovirus-transduced insect cells, purified and crystallized to yield a 0.98 Å resolution unliganded structure and a trapped covalent intermediate structure with 2-deoxy-2-fluoro-β-D-glucopyranoside.

This work demonstrates the use of a broad energy bandwidth multilayer mirror monochromator for X-ray total scattering (TS) measurements and pair distribution function (PDF) analysis. This type of measurement could facilitate faster time-resolved TS and PDF studies.

Fresnel zone plates for nano-ARPES in the extreme ultraviolet regime have been fabricated and tested. The optics provide high photon flux combined with spot sizes down to 0.4 µm.

With the currently avalaible 3D ED data it is possible to observe details of electrostatic potential deformations due to chemical bonding in organic crystals. The deformation signal is strong enough to see the benefits of using a more accurate potential model (TAAM) in achieving a better fit of the model to the experimental data.

A 0.27 meV-bandwidth monochromator for 21.5 keV synchrotron radiation demonstrates exceptional stability using cryogenic stabilization and active feedback control.

A near-atomic resolution map was obtained for lumazine synthase while benchmarking a new microscope. At this resolution, waters, ligands and hydrogens were visible. A detailed outline of the methods used is presented that can employed for any single-particle cryo-EM experiment.

Details of five very high-resolution accurate structures of bovine trypsin are compared in the context of the reproducibility of models obtained from crystals grown under identical conditions.