forthcoming articles

We report the X-ray crystal structure of Omp33 at a resolution of 2.1 Å. The structure helps us to understand how A. baumannii OM proteins contribute to the low permeability of the cell envelope and suggests it may function as a ligand-gated channel.

The complete post-fusion core structure of the HCoV-229E spike protein was determined at 1.86 Å. Comparison of the interactions between HR1 and HR2 in different human coronaviruses reveals some differences, which should be taken into consideration when designing pan-CoVs HR2 mimic inhibitors that target HR1.

Analysis of intermolecular interactions in the crystal structures of G protein-coupled receptors showed two major types of dimers.

A high-resolution crystal structure of a pan-specific synthetic Fab selected using a phage-display system against the C-terminal domain of the nucleoprotein from the Ebola virus is reported.

The biochemical and crystallographic characterization of different Catharanthus roseus receptor kinase 1-like membrane receptors is reported as a first step to understand cell-wall sensing and signalling mechanisms in plants.

A high-resolution X-ray structure of the seventh FAS1 domain of stabilin-2 is presented. This structure provides the first insight into the structure of stabilin-2.

Small-angle neutron scattering is coupled with on-line size exclusion chromatography. The obtained SEC-SANS is combined with SEC-SAXS and utilized to investigate solution structures of phospholipid nanodiscs with and without membrane proteins incorporated.

The crystal structure of the complex between a substrate selected by phage display and the D25N variant of HIV-1 protease is reported at a resolution of 1.1 Å. The structure has several unprecedented features, especially the formation of additional hydrogen bonds between the enzyme and the substrate.

The engineering of metal binding into a cellulase increases its temperature stability while maintaining its other catalytic properties.

The application of protein X-ray crystallography cryogenic data collection environments for neutron protein crystallography is discussed.

First-principles signal-to-noise calculations for BioSAXS have been developed and applied to evaluate the impact of energy, source brightness, window scattering and other variables on the ability to detect and distinguish protein conformational changes.

Small-angle neutron scattering (SANS) provides structural information on biological macromolecules in solution that is perfectly complementary to the information obtained by other structural biology techniques, including crystallography, nuclear magnetic resonance and electron microscopy. Compared with its sister technique SAXS (small-angle X-ray scattering), SANS allows specific and individual information to be obtained on subunits within important heterogeneous biological assemblies such as multiprotein or protein–RNA/DNA complexes as well as solubilized membrane proteins.

To improve the sensitivity of hydrogen detection using neutrons, high-pressure freezing of a relatively large protein single crystal and the proton polarization of a protein polycrystalline state were demonstrated as preliminary experiments.

Using the unique ability of small-angle neutron scattering to resolve a hydrogen-rich surfactant from a deuterated membrane protein, the results of removing free surfactant from the equilibrium are revealed.

Recent work applying neutron and X-ray scattering to elucidate molecular mechanisms of volatile anesthetics is reviewed

Models of crystal structures determined by neutron diffraction deposited in the Protein Data Bank to date were analysed. Lessons learned from this data-mining effort are summarized and suggestions for improvements to the deposition and validation of neutron models are outlined.