An imaging technique pioneered by Berkeley Lab is helping reveal the best antibodies to test for in rapid and reliable COVID-19 detection. Although current tests such as polymerase chain reaction (PCR) are highly accurate, these samples must be sent to an accredited lab for testing, causing a longer wait time for results. Michal Hammel, a research scientist in the Molecular Biophysics and Integrated Bioimaging Division, and Curtis D. Hodge led a study that could help get reliable, self-administered tests with instant results on the market.
In a study appearing in Nature Plants, researchers from UC Davis, UC Berkeley, and Berkeley Lab report the discovery and characterization of a previously undescribed lineage of form I rubisco – one that the researchers suspect diverged from form I rubisco prior to the evolution of cyanobacteria. The novel lineage, called form I’ rubisco, gives researchers new insights into the structural evolution of form I rubisco, potentially providing clues as to how this enzyme changed the planet.
The work was led by Patrick Shih, a UC Davis assistant professor and the director of Plant Biosystems Design at the Joint BioEnergy Institute (JBEI), and Doug Banda, a postdoctoral scholar in his lab.
A Berkeley Lab-led team of researchers used multiple high-powered X-ray techniques at the Advanced Light Source to image the process in E. coli bacteria at the micro-, meso-, and nanoscales. The imaging technique they developed enabled them to visualize the bacteria’s chromosome at higher resolutions than ever before, and without the need for labeling, which slows down the process but is required by most other techniques.
Bioscientists at the Advanced Light Source (ALS) at Berkeley Lab lent their expertise to a project led by scientists at the University of Washington to design proteins in the lab that zip together like DNA. The technique could enable the design of protein nanomachines to help diagnose and treat disease, allow for more precise engineering of cells, and perform a variety of other tasks.
Structurally Integrated Biology for Life Sciences (SIBYLS) beamline researchers, led by research scientist Michal Hammel of the Molecular Biophysics & Integrated Bioimaging (MBIB) Division, used X-ray scattering to define an unexpected key role for unfolded protein regions in DNA break repair to allow regulation plus access to DNA ends. The concept of DNA break repair as a flexibly-linked dynamic complex, as opposed to a linear pathway, suggests new approaches to targeting DNA repair for selectively killing cancer cells due to their high levels of DNA instability. Their findings were published in a recent cover article of the Journal of Biological Chemistry.
The SIBYLS beamline of the Advanced Light Source at Berkeley Lab, directed by MBIB’s senior scientist John Tainer, is optimized for both small-angle X-ray scattering (SAXS) and macromolecular crystallography (MX), making it unique among the world’s mostly SAXS or MX dedicated beamlines.