In his blog late last week, NIH Director Francis S. Collins highlighted Cryo-EM Microscopy, the Method of the Year 2015. Collins gave a retrospective analysis of how far the method has come over the past decade, and credits most of the advances to improvements in the technology available, particularly computational methods for image construction and direct electron detectors that can fix the blurring problem caused by molecules moving around in the electron beam. With these and other changes, the number of structures determined using this method have increased substantially in just the past year. Molecular Biophysics & Integrated Bioimaging’s Robert Glaeser got a shout-out for his Nature Methods commentary, which says that owing to the laws of physics, we can expect more good things.
Seeing the Big Picture in Photosynthetic Light Harvesting
Graham Fleming, chemist senior faculty scientist in Molecular Biophysics & Integrated Bioimaging, led the creation of the first computational model that simulates the light-harvesting activity of the thousands of antenna proteins that would be interacting in the chloroplast of an actual leaf. The results from this model point the way to improving the yields of food and fuel crops, and developing artificial photosynthesis technologies. Read more at Berkeley Lab News Center.
Big Moves in Protein Structure Prediction and Design
The potential of modular design for brand new proteins that do not yet exist in the natural world are the latest in a recent series of developments toward custom-designing proteins. Scientists with the University of Washington used the Berkeley Lab Advanced Light Source (ALS) for some of their research. They collaborated with Susan Tsutakawa , Greg Hura, and Kathryn Burnett, of the Molecular Biophysics & Integrated Bioimaging Division, who work at the ALS beamline SIBYLS where some crystallography studies of repeat protein molecule structures took place.
Single-Particle Cryo-Electron Microscopy Named Method of the Year
Nature Methods recognized the technology for “its newfound ability to determine challenging protein and protein-complex structures at high resolution.” In the journal, the Lab’s Eva Nogales and Robert Glaeser comment on cryo-EM and technological advancements that provide near-atomic resolutions of protein structures without the need for crystallization. The announcement has links to the Nogales and Glaeser Commentaries.
Nature’s Microscopic Masonry: The First Steps in How Thin Protein Sheets Form Polyhedral Shells
Scientists for the first time have viewed how bacterial proteins self-assemble into thin sheets and begin to form the walls of the outer shell for nano-sized polyhedral compartments that function as specialized factories. Researchers in the Molecular Biophysics & Integrated Bioimaging Division determined the 3-D structure of the basic building block protein from crystallized samples in the Berkeley Center for Structural Biology at the Advanced Light Source. Their findings may eventually help improve drug delivery systems. Read more in the Berkeley Lab News Center.
- « Previous Page
- 1
- …
- 70
- 71
- 72
- 73
- 74
- 75
- Next Page »
Was this page useful?