A team led by Harald Hess at the Howard Hughes Medical Institute (HHMI) Janelia Research Campus and Eric Betzig, a senior faculty scientist in the Molecular Biophysics and Integrated Bioimaging (MBIB) Division, has devised a technique that combines cryogenic super-resolution fluorescence microscopy and focused ion beam–milling scanning electron microscopy. In a report in the journal Science, the researchers describe their technique, called cryo-SR/EM, and display some of exquisitely detailed three-dimensional images they captured of the complex innards of cells.
Berkeley Lab scientists have demonstrated for the first time that cryogenic electron microscopy (cryo-EM), a Nobel Prize-winning technique originally designed to image proteins in solution, can be adapted to image atomic changes in a synthetic soft material.
Researchers led by Ivaylo Ivanov of Georgia State University have produced a comprehensive model of the human transcription preinitiation complex (PIC), a vital assembly of proteins responsible for regulating gene expression. The new model is the most complete to date and provides mechanistic insights into how mutations affecting one component—human transcription initiation factor IIH, or TFIIH—lead to three inherited genetic diseases. Berkeley Lab Biosciences’ Susan Tsutakawa, a research scientist in Molecular Biophysics and Integrated Bioimaging (MBIB), and John Tainer, a professor at the University of Texas MD Anderson Cancer Center and visiting faculty in MBIB, were part of the team. Results from this work were recently published in Nature Structural & Molecular Biology.
To better understand how coronavirus antibodies work, a team of researchers at the University of Washington studied spike protein structures in complex with neutralizing antibody fragments isolated from SARS and MERS survivors. To visualize how the spike structures interact with the antibody fragments, they used a cryo-electron microscopy (cryo-EM) for the spikes, which are resistant to crystallization, and protein crystallography for the fragments. The high-resolution x-ray crystallography was performed at the Advanced Light Source (ALS) Beamline 5.0.1, part of the Berkeley Center for Structural Biology (BCSB).
A team of scientists from the Molecular Biophysics and Integrated Bioimaging (MBIB) Division and UC Berkeley has constructed the first complete atomic blueprint of a complicated molecular machine that is crucial to repairing and reading DNA. These protein assemblies, human transcription initiation factor IIH (TFIIH), are essential to survival, yet we know little about how they function because, until recently, it was impossible to accurately describe their structure.