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Electro-Active Tech license signing ceremony

Electro-Active Technologies, Inc., of Knoxville, Tenn., has exclusively licensed two biorefinery technologies invented and patented by the startup’s co-founders while working at the Department of Energy’s Oak Ridge National Laboratory. The technologies work as a system that converts organic waste into renewable hydrogen gas for use as a biofuel.

early prototype of the optical array developed by Oak Ridge National Laboratory.

IDEMIA Identity & Security USA has licensed an advanced optical array developed at Oak Ridge National Laboratory. The portable technology can be used to help identify individuals in challenging outdoor conditions.

Stephanie Galanie

Early career scientist Stephanie Galanie has applied her expertise in synthetic biology to a number of challenges in academia and private industry. She’s now bringing her skills in high-throughput bio- and analytical chemistry to accelerate research on feedstock crops as a Liane B. Russell Fellow at Oak Ridge National Laboratory.

Laccaria bicolor is fruiting aboveground and colonizing the Populus deltoides plant root system belowground in a greenhouse setting.

A team of scientists led by Oak Ridge National Laboratory have discovered the specific gene that controls an important symbiotic relationship between plants and soil fungi, and successfully facilitated the symbiosis in a plant that

Alex Johs at ORNL's Spallation Neutron Source

Sometimes solutions to the biggest problems can be found in the smallest details. The work of biochemist Alex Johs at Oak Ridge National Laboratory bears this out, as he focuses on understanding protein structures and molecular interactions to resolve complex global problems like the spread of mercury pollution in waterways and the food supply.

Strain-tolerant, triangular, monolayer crystals of WS2 were grown on SiO2 substrates patterned with donut-shaped pillars, as shown in scanning electron microscope (bottom) and atomic force microscope (middle) image elements.

A team led by scientists at the Department of Energy’s Oak Ridge National Laboratory explored how atomically thin two-dimensional (2D) crystals can grow over 3D objects and how the curvature of those objects can stretch and strain the 

Pictured in this early conceptual drawing, the Translational Research Capability planned for Oak Ridge National Laboratory will follow the design of research facilities constructed during the laboratory’s modernization campaign.

OAK RIDGE, Tenn., May 7, 2019—Energy Secretary Rick Perry, Congressman Chuck Fleischmann and lab officials today broke ground on a multipurpose research facility that will provide state-of-the-art laboratory space 

ORNL collaborator Hsiu-Wen Wang led the neutron scattering experiments at the Spallation Neutron Source to probe complex electrolyte solutions that challenge nuclear waste processing at Hanford and other sites. Credit: Genevieve Martin/Oak Ridge National Laboratory, U.S. Dept. of Energy.

Researchers at the Department of Energy’s Oak Ridge National Laboratory, Pacific Northwest National Laboratory and Washington State University teamed up to investigate the complex dynamics of low-water liquids that challenge nuclear waste processing at federal cleanup sites.

Molecular dynamics simulations of the Fs-peptide revealed the presence of at least eight distinct intermediate stages during the process of protein folding. The image depicts a fully folded helix (1), various transitional forms (2–8), and one misfolded state (9). By studying these protein folding pathways, scientists hope to identify underlying factors that affect human health.

Using artificial neural networks designed to emulate the inner workings of the human brain, deep-learning algorithms deftly peruse and analyze large quantities of data. Applying this technique to science problems can help unearth historically elusive solutions.

Illustration of the intricate organization of the PKA structure, wherein different parts of the protein are connected through elaborate hydrogen bonding networks (dashed yellow lines), glued together by the hydrophobic assemblies (light blue and orange volumes)—all working together to build the functional active site. Insert shows protonation of the transferred phosphoryl group (cyan mesh) and its many interactions with water and the active site amino acid residues. Credit: Jill Hemman/ORNL

OAK RIDGE, Tenn., March 20, 2019—Direct observations of the structure and catalytic mechanism of a prototypical kinase enzyme—protein kinase A or PKA—will provide researchers and drug developers with significantly enhanced abilities to understand and treat fatal diseases and neurological disorders such as cancer, diabetes, and cystic fibrosis.