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.
The combination of bioenergy with carbon capture and storage could cost-effectively sequester hundreds of millions of metric tons per year of carbon dioxide in the United States, making it a competitive solution for carbon management, according to a new analysis by ORNL scientists.
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.
Gina Tourassi has been appointed as director of the National Center for Computational Sciences, a division of the Computing and Computational Sciences Directorate at Oak Ridge National Laboratory.
Researchers at the Department of Energy’s Oak Ridge National Laboratory have received five 2019 R&D 100 Awards, increasing the lab’s total to 221 since the award’s inception in 1963.
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.