Willy Wriggers
Old Dominion University, VA·Biophysics
Cryo-electron microscopy can now reveal the shapes of large molecular machines in fine detail. Deep learning tools such as AlphaFold can also predict the atomic structures of proteins.
- Fields
Biophysics
Computer Science
Biochemistry
- Topics
cryo-electron microscopy
cryo-EM
cryo-electron tomography
- Grants
- 1 known grant, through Aug 2029
What they work on
- Develop measures of how well an atomic model fits local regions of a cryo-electron microscopy (cryo-EM) density map, and rate maps against reliable reference structures.
- Improve flexible fitting and refinement of AlphaFold2-predicted atomic models into cryo-EM maps, and predict secondary structure (helices and sheets) in medium-resolution maps.
- Build a software tool that simulates realistic "phantom" cryo-electron tomography (cryo-ET) maps with a known true structure, and use it to validate methods that trace cytoskeletal filaments.
- Apply the methods with collaborators to refine actin filaments, molecular motors, bacterial chemoreceptor arrays and hair-cell stereocilia, and distribute them through Situs, Sculptor and UCSF Chimera plugins.
More about the research
Many images still come out blurry or noisy, though, especially when molecules are imaged inside cells. Researchers need reliable computer methods to fit atomic models into these imperfect 3D maps and to check whether the fits can be trusted.
Why it matters
Macromolecular assemblies are the basic working units of cells, and defects in how they are built are often linked to disease, which makes them targets for drug design. Free, validated software for modeling these structures could help electron microscopists across biology interpret their maps more reliably. This could support structure-based work on drug targets.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
Salim Sazzed
Georgia Southern University, GA·Computer Science
Characterize the structural inconsistencies and variability of protein secondary structures, such as helices and sheets, in medium-resolution cryo-electron microscopy (cryo-EM) maps.
Gregory Alushin
Rockefeller University, NY·Biophysics
Determine the structural mechanisms and cellular functions of catch bonds, protein contacts that strengthen under pulling force, in cytoskeletal crosslinking proteins and cell adhesion proteins implicated in force sensing.
Maria Lara-Tejero
Yale University, CT·Microbiology & Immunology
Determine the structure of the Salmonella type III secretion sorting platform, the part of the injectisome inside the bacterium, using cryo-EM and cryo-electron tomography.
The school
Old Dominion University: 8 labs on PI Pages, $76M a year on research, 143 research doctorates a year.
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