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<p>The high-resolution crystal structure of one of the proteins studied, a computationally designed trimer. The structure has been deposited in the Protein Data Bank with accession number 5HRZ.</p>

Designing Cyclic Oligomers: Greater Than the Sum of Their Parts

-Written By Lida Gifford Cyclic proteins that assemble from multiple identical subunits (homo-oligomers) play key roles in many biological processes, including cell signaling and enzymatic catalysis and protein function. Researchers in Berkeley Lab’s Molecular Biophysics and Integrated Bioimaging (MBIB) Division worked with University of Washington’s David Baker, who led a team to design in silico

<p>Complete capsid of bacteriophage P22 generated with validated atomic models that were derived from a high-resolution cryo-electron microscopy density map. (C. Hryc and the Chiu Lab, Baylor College of Medicine)</p>

Cryo-Electron Microscopy Achieves Unprecedented Resolution Using New Computational Methods

Cryo-electron microscopy (cryo-EM)—which enables the visualization of viruses, proteins, and other biological structures at the molecular level—is a critical tool used to advance biochemical knowledge. Now Lawrence Berkeley National Laboratory (Berkeley Lab) researchers have extended cryo-EM’s impact further by developing a new computational algorithm that was instrumental in constructing a 3-D atomic-scale model of bacteriophage