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Media Contacts
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.
Oak Ridge National Laboratory has licensed a novel method to 3D print components used in neutron instruments for scientific research to the ExOne Company, a leading maker of binder jet 3D printing technology.
A team led by the Department of Energy’s Oak Ridge National Laboratory synthesized a tiny structure with high surface area and discovered how its unique architecture drives ions across interfaces to transport energy or information.
Scientists have found a new method to strategically add deuterium to benzene, an aromatic compound commonly found in crude oil. When applied to the active ingredient of drugs to incorporate deuterium, it could dramatically improve the drugs’ efficacy and safety and even introduce new medicines.
Oak Ridge National Laboratory researchers working on neutron imaging capabilities for nuclear materials have developed a process for seeing the inside of uranium particles – without cutting them open.
An international team of scientists, led by the University of Manchester, has developed a metal-organic framework, or MOF, material
Researchers used neutron scattering at Oak Ridge National Laboratory’s Spallation Neutron Source and High Flux Isotope Reactor to better understand how certain cells in human tissue bond together.
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.