Robert Glaeser, senior scientist in the Molecular Biophysics & Integrated Bioimaging Division, was awarded the Glenn T. Seaborg Medal by the Department of Chemistry & Biochemistry at the University of California, Los Angeles (UCLA). At a symposium held on November 1o, Glaeser and Richard Henderson, Nobel Laureate in Chemistry 2017, were recognized for their “crucial contributions to the science of electron cryo-microscopy.”
Photosynthesis, Like a Moss
Using cryo-electron microscopy (cryo-EM), which allows an unprecedented level of resolution, Biosciences researchers compared the structure of photosystem I in the moss Physcomitrella patens with its structure in the small flowering land plant Arabidopsis thaliana, and in the green alga Chlamydomonas reinhardtii. Because moss evolved after algae but before vascular land plants, such comparisons can shed light on how plants evolved to move from the ocean to land.
Biosciences’ Kenneth H. Downing Passes Away
The Berkeley Lab community mourns the loss of Kenneth H. Downing, who died August 2 at age 72. A senior scientist in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division, Downing worked at the Lab for more than four decades. He passed away at home, surrounded by his family. A memorial service will be held on Saturday, September 1, at 11:00 a.m. at Lafayette Orinda Presbyterian Church, with a reception to follow.
Tau-tally Microtubular: A Structural Model of Tau-Microtubule Interaction
Researchers at Berkeley Lab and UC Berkeley have combined cutting-edge cryo-electron microscopy (cryo-EM) with computational molecular modeling to produce a near atomic-resolution model of the interaction between microtubules—crucial components of eukaryotic cell ultrastructure—and microtubule-associated proteins called tau. The model provides insight into how tau stabilizes microtubules, and what makes it dissociate to form tau aggregates, or “tangles,” in some neurological diseases—including Alzheimer’s disease—generally referred to as tauopathies.
Cryo-EM Reveals Structure of Human Telomerase
Regulation of the enzyme telomerase has been implicated in cancer, other human diseases, and aging, but progress towards therapeutic manipulation of telomerase has been hampered by the lack of high-resolution structural data. Now, researchers in senior faculty scientist Eva Nogales’ lab in Molecular Biophysics and Integrated Bioimaging (MBIB), in collaboration with UC Berkeley professor of Biochemistry, Biophysics and Structural Biology Kathleen Collins, have published a paper in Nature describing the 3-D molecular structure of the human telomerase enzyme.
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