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Media Contacts
![Distinguished Inventors](/sites/default/files/styles/list_page_thumbnail/public/2020-12/inventors.jpg?h=4631f1c1&itok=xhAGY0kv)
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. Credit: ORNL, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2020-11/AAASfellows.jpg?h=d761c044&itok=opKRkA17)
Six ORNL scientists have been elected as fellows to the American Association for the Advancement of Science, or AAAS.
![The first neutron structure of the SARS-CoV-2 main protease enzyme revealed unexpected electrical charges in the amino acids cysteine (negative) and histidine (positive), providing key data about the virus’s replication. Credit: Jill Hemman/ORNL, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2020-10/20-G01620_Protease_PR_proof2_0.jpg?h=3e3883a3&itok=XB_ZEDFQ)
To better understand how the novel coronavirus behaves and how it can be stopped, scientists have completed a three-dimensional map that reveals the location of every atom in an enzyme molecule critical to SARS-CoV-2 reproduction.
![The protease protein is both shaped like a heart and functions as one, allowing the virus replicate and spread. Inhibiting the protease would block virus reproduction. Credit: Andrey Kovalevsky/ORNL, U.S. Dept. of Energy](/sites/default/files/styles/list_page_thumbnail/public/2020-06/protease_dimer_3_1.png?h=aa51a450&itok=sJY7AB8d)
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.
![Batteries - The 3D connection](/sites/default/files/styles/list_page_thumbnail/public/2020-05/Batteries_3D%20story%20tip_2.jpg?h=aeb34e32&itok=puhZ_584)
Oak Ridge National Laboratory researchers have developed a thin film, highly conductive solid-state electrolyte made of a polymer and ceramic-based composite for lithium metal batteries.
![Representatives from The University of Toledo and the U.S. Department of Energy’s Oak Ridge National Laboratory (ORNL) in Tennessee are teaming up to conduct collaborative automotive materials research.” Credit: University of Toledo](/sites/default/files/styles/list_page_thumbnail/public/2019-10/Oak%20Ridge%20Nat%20Lab%20group%20photo_0.jpeg?h=1e7f2295&itok=pITK15-V)
ORNL and The University of Toledo have entered into a memorandum of understanding for collaborative research.
![Salting the gears](/sites/default/files/styles/list_page_thumbnail/public/2019-09/Salting-the-gears_1_0.png?h=b00637a2&itok=gsk3DeGh)
Researchers at Oak Ridge National Laboratory proved that a certain class of ionic liquids, when mixed with commercially available oils, can make gears run more efficiently with less noise and better durability.
![Tungsten tiles for fusion](/sites/default/files/styles/list_page_thumbnail/public/2019-07/EBM-tungsten_tiles_ORNL.png?h=0c890573&itok=XgIsl0tA)
Using additive manufacturing, scientists experimenting with tungsten at Oak Ridge National Laboratory hope to unlock new potential of the high-performance heat-transferring material used to protect components from the plasma inside a fusion reactor. Fusion requires hydrogen isotopes to reach millions of degrees.
![Batteries—Polymers that bind](/sites/default/files/styles/list_page_thumbnail/public/2019-06/Batteries-Polymers_that_bind_0.png?h=dec22bcf&itok=oJ7mroY1)
A team of researchers at Oak Ridge National Laboratory have demonstrated that designed synthetic polymers can serve as a high-performance binding material for next-generation lithium-ion batteries.
![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](/sites/default/files/styles/list_page_thumbnail/public/2019-03/19-G00204_MR_graphic_Kovalevsky_proof5_2.png?h=b7fbb1a9&itok=wrZFNX-o)
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.