A wide variety of neutron scattering techniques can be applied to obtain information on the structure and dynamics of biological systems on multiple scales. Recent progress is summarized, as are hoped-for future developments in the context of the advent of next-generation neutron sources on various continents.

By installing calcium-ligand triads found in olfactomedin sequences from invertebrates, insight was gained into calcium-binding features across the protein family and new surface conformations were observed that may be relevant to elusive protein–protein interactions.

A Fab fragment with nanomolar affinity for the peptide sequence EYMPME was engineered and characterized by structural, biophysical and computational methods for potential use as a membrane-protein crystallization chaperone.

Contrary to expectation from orthologous structures from mouse and cow, a structure of holo human adenosine deaminase 1 shows that it adopts a closed conformation at the entry to its active site. This finding poses a cautionary tale for reliance on homologs to make structural inferences relevant to applications such as protein engineering or drug development.

Crystals of actophorin were grown in microgravity in an interactive process with astronauts on the International Space Station. Although the diffraction was not improved compared with crystals grown on Earth, a conformational change suggestive of motions intrinsic to actophorin function was observed.

Site-directed mutants of the actin filament-severing protein actophorin were produced to improve the crystal size and diffraction limit. When 19 single mutants and a C-terminal three-residue deletion were combined into one variant, the resulting protein was significantly more thermostable and slightly more active than the wild-type protein. Larger crystals were obtained that diffracted to 1.7 Å resolution and belonged to a different space group to previous actophorin crystals.