A team based at Berkeley Lab’s Advanced Light Source is making waves with its new approach for whole-cell visualization, using the world’s first soft X-ray tomography (SXT) microscope built for biological and biomedical research. In its latest study, published in Science Advances, the team used its platform to reveal never-before-seen details about insulin secretion in pancreatic cells taken from rats. This work was done in collaboration with a consortium of researchers dedicated to whole-cell modeling, called the Pancreatic β-Cell Consortium.
Get a Move On: Protein Translates Chemistry into Motion
The protein CheY plays a role in relaying sensory signals from chemoreceptors to the rotary motor at the base of the tail-like appendage, or flagellum, that protrudes from the cell body of certain bacteria and eukaryotic cells. It has been studied as a model for dissecting the mechanism of allostery—the process by which the binding of biological macromolecules (mainly proteins) at one location regulates activity at another, often distant, functional site. When it is transiently phosphorylated in response to chemotactic cues, CheY’s binding affinity for a flagellar motor switch protein called FliM is enhanced. CheY binding to FliM changes the direction of flagellar rotation from counterclockwise to clockwise.
Using X-ray footprinting with mass spectroscopy (XFMS), a team led by Shahid Khan, a senior scientist with the Molecular Biology Consortium, established that CheY changes shape when it tethers to the motor, and further parsed the contribution of phosphorylation to this shape change. The results of the XFMS experiments validated atomistic molecular dynamics (MD) predictions of the architecture of the allosteric communication network, marking the first time that XFMS has been used to validate protein dynamics simulations at single-residue resolution sampled over the complete protein.
Experimental Drug Targets HIV in a Novel Way
Using Berkeley Center for Structural Biology (BCSB) beamline 5.0.1, researchers from Gilead Sciences investigated a promising small-molecule drug, GS‑6207, that they developed to inhibit replication of the human immunodeficiency virus (HIV).
Jennifer Doudna and the Nobel Prize: The Advanced Light Source Perspective
Emmanuelle Charpentier and Jennifer Doudna winning the 2020 Nobel Prize for Chemistry for their development of the CRISPR method of genome editing is a momentous achievement, supported by the contributions of numerous individuals and institutions, including the Advanced Light Source (ALS) synchrotron user facility at Berkeley Lab. This feature details how Doudna’s research was enabled by the facility’s early embrace of hard X-ray crystallography technology for atomic-level understanding of molecular structure, as well as her use of the Berkeley Center for Structural Biology’s (BCSB’s) wiggler-based beamline 5.0.2 for macromolecular crystallography. Doudna has published some 35 papers using ALS crystallography beamlines, including two cited by the Nobel Committee in its CRISPR-Cas9 scientific background document.
Focusing in on Aquatic Microbes: Berkeley Lab Scientists Receive Grant for New Microscopy Approach
The Gordon and Betty Moore Foundation is supporting the development of a unique microscopy concept pioneered by researchers at Berkeley Lab as part of the Foundation’s Symbiosis in Aquatic Systems Initiative (SASI). The Berkeley Lab effort has received $500,000 and will be led by senior staff scientist Hoi-Ying Holman of the Molecular Biophysics and Integrated Bioimaging (MBIB) Division.
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