Biosciences Area

New Algorithm Sharpens Focus of World’s Most Powerful Microscopes

In recent years, cryo-electron microscopy (cryo-EM) technology has advanced to the point that it can produce structures with atomic-level resolution for many types of molecules. Yet in some situations, even the most sophisticated cryo-EM methods still generate maps with lower resolution and greater uncertainty than required to tease out the details of complex chemical reactions.

In a study published in Nature Methods, a multi-institutional team led by Tom Terwilliger from the New Mexico Consortium and including researchers from Berkeley Lab demonstrates how a new computer algorithm improves the quality of the 3D molecular structure maps generated with cryo-EM.

New Microscopy Technique Gives Detailed 3D View Inside Cells

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.

Researchers Create Comprehensive Model of Transcription Preinitiation Complex

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.

Antibody Uses Mimicry to Block SARS Coronavirus

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).

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