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.
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Apr 30, 2021 - 2021 APS/CNM Joint Virtual Users Meeting – May 3-14