Vukica Srajer
University of Chicago, IL·Biophysics
A protein structure solved by crystallography is a snapshot, but proteins work by moving. Those internal motions, small shifts of loops and side chains over timescales relevant to function, are what actually carry out catalysis, signaling, and binding, and they are far harder to see than static shapes.
- Fields
Biophysics
Biochemistry
Physics
- Topics
X-ray crystallography
protein dynamics
time-resolved crystallography
- Grants
- 1 known grant, through May 2030
What they work on
- Install and test new hardware to generalize Electric-Field Stimulated X-ray crystallography, in which strong external electric fields induce motions in protein crystals that are then recorded by X-ray diffraction at atomic resolution.
- Calibrate the magnitude and orientation of the forces that applied electric fields exert at specific local environments within biological macromolecules, so that observed motions can be interpreted quantitatively.
- Build a modern, open-source, end-to-end software pipeline for reducing and analyzing raw electric-field-stimulated diffraction data and for simplifying biological interpretation of the resulting motions.
- Advance computational simulations that pair with the experiments in an iterative cycle, filling gaps in and extending the experimental analysis of intramolecular protein dynamics.
More about the research
Being able to watch them directly would change how researchers explain biological function in health and disease, engineer new activities into proteins, and design drugs rationally.
Why it matters
Explaining how a protein functions, or why a mutation causes disease, often requires knowing how the molecule moves rather than only what it looks like at rest. By turning Electric-Field Stimulated X-ray crystallography into a usable general method with open-source analysis software, this work could give the wider research community a practical route to atomic-resolution movies of macromolecular machinery, which may inform protein engineering and structure-based drug design.
Known grants
From NIH and NSF research grants. Labs often have other funding we can't see.
Closest labs
James Solomon Fraser
University of California-San Francisco, CA·Biophysics
Improve computational methods for finding and modeling alternative protein shapes in cryoEM density maps, extending the multiconformer modeling the group built for X-ray crystallography.
Malcolm Capel
Cornell University, NY·Biophysics
Provide and staff round-the-clock on-site and remote user access to two macromolecular crystallography beamlines at the Advanced Photon Source, including training and outreach by staff scientists.
Galina Lepesheva
Vanderbilt University, TN·Biochemistry
Determine how large-scale shape changes guide CYP51, the sterol-making enzyme targeted by antifungal drugs, through each step of its three-step reaction, using X-ray crystallography, cryo-electron microscopy and computational approaches.
The school
University of Chicago: 39 labs on PI Pages, $681M a year on research, 457 research doctorates a year.
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