Using neutrons to see the additive manufacturing process at the atomic level, scientists have shown that they can measure strain in a material as it evolves and track how atoms move in response to stress.
Laboratory Director Thomas Zacharia presented five Director’s Awards during Saturday night's annual Awards Night event hosted by UT-Battelle, which manages ORNL for the Department of Energy.
ORNL scientists will present new technologies available for licensing during the annual Technology Innovation Showcase. The event is 9 a.m. to 3 p.m. Thursday, June 16, at the Manufacturing Demonstration Facility at ORNL’s Hardin Valley campus.
In the quest for advanced vehicles with higher energy efficiency and ultra-low emissions, ORNL researchers are accelerating a research engine that gives scientists and engineers an unprecedented view inside the atomic-level workings of combustion engines in real time.
Six scientists at the Department of Energy’s Oak Ridge National Laboratory were named Battelle Distinguished Inventors, in recognition of obtaining 14 or more patents during their careers at the lab.
Six ORNL scientists have been elected as fellows to the American Association for the Advancement of Science, or AAAS.
Five researchers at the Department of Energy’s Oak Ridge National Laboratory have been named ORNL Corporate Fellows in recognition of significant career accomplishments and continued leadership in their scientific fields.
Scientists at ORNL used neutron scattering and supercomputing to better understand how an organic solvent and water work together to break down plant biomass, creating a pathway to significantly improve the production of renewable
A team of researchers has performed the first room-temperature X-ray measurements on the SARS-CoV-2 main protease — the enzyme that enables the virus to reproduce.
Using the Titan supercomputer and the Spallation Neutron Source at the Department of Energy’s Oak Ridge National Laboratory, scientists have created the most accurate 3D model yet of an intrinsically disordered protein, revealing the ensemble of its atomic-level structures.