forthcoming articles

Sub-atomic X-ray structures of green fluorescent protein

Thus, the expanding 'tool-kit' of structural biology with further advances in technologies associated with cryoEM, synchrotron and XFEL, and 'ease of their use' would continue to enable the wider community to address more complicated and demanding scientific questions ensuring the 'pole-position' of structural biology.

Nanoconfinement dramatically modifies the behaviour of solvent within protein crystals, allowing biophysical measurements in the presence of liquid solvent at temperatures down to ~200 K. When internal ice forms it is stacking disordered, consistent with nucleation within deeply supercooled solvent, and ice does not form in solvent within ~5 Å of the protein surface.

X-ray free-electron lasers were used for single-particle imaging of 3D nanoscale structures. Through the extraction of single-particle diffraction patterns from the data, the performances of image-classification algorithms were evaluated and the final reconstruction results depended on the selection of dataset.

The co-crystal structure of the metallopeptidase astacin with its specific protein inhibitor fetuin-B reveals a novel mechanism of inhibition.

The combination of oscillation data collection with fixed-target microchips for regular crystal dispersion is an efficient method for collecting serial crystallography data at synchrotrons. Background scatter from noncrystal substrates is especially minimized.

The short- and long-range order of thin films with thicknesses down to 3 nm were studied by applying PDF analysis to data collected by surface high-energy X-ray diffraction at a time resolution on the scale of seconds.