Overview

Structures of dirigent proteins (DPs) and enzymes with DP-like domains advance efforts to understand the biochemical roles DPs play in the coupling reactions leading to important plant compounds.

Multiscale X-ray techniques shed light on interactions between Escherichia coli DNA and the DNA-binding protein HU, which could eventually inform strategies to control microbial behavior.

Neutron scattering and molecular simulations reveal effects of tetrahydrofuran-water pretreatment on the nanoscale architecture of plant biomass.

New technique uses lanthanide-binding tags and X-ray fluorescence to image proteins in three dimensions with nanoscale resolution.

Team discovers ancient form of the enzyme and uses x-ray crystallography and small-angle X-ray scattering data to study how its structure changes during different activities.

X-ray and cryo-electron microscopy reveal the structure of Hsp104, a fungal protein known as a chaperone, which helps the natural folding processes of proteins for proper cell function.