BER Structural Biology and Imaging Resources
Synchrotron, Neutron, and Cryo-EM
U.S. Department of Energy | Office of Science | Office of Biological and Environmental Research

Mission

World-class structural biology and imaging resources supported by DOE’s Office of Biological and Environmental Research (BER) enable scientists to functionally characterize plant and microbial systems across a range of space and time scales. These enabling capabilities, together with cutting-edge genomic science approaches, are underpinning advances in BER’s bioenergy, biosystems design, environmental microbiome, and environmental system science research.

Research Themes

Molecular Structure

Cell & Tissue Structure

Chemical Elemental Information

Chemical & Elemental Information

Highlights

Phenoxy Radical-Radical Coupling in Plants

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.

How Proteins Remodel DNA in Bacteria under Stress

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.

Role of Solvents in Efficient Biomass Deconstruction

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

Cell Membrane Proteins Imaged in 3D

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

“Missing Link” in Evolutionary History of the Carbon-Fixing Protein Rubisco

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.

Protein Chaperones

Breakthrough Shines Light on Protein Chaperones

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.