Macromolecules rarely operate in isolation inside cells. At any given time, the average protein is part of a complex of over 10 macromolecules, and these supramolecular complexes are in turn embedded in intricate networks inside cells. We are broadly interested in revealing the structure and function of macromolecular complexes in their natural environment at the highest possible resolution in order to reveal their structural dynamics and interactions. We call it bringing structure to cellular biology.

Method Development
Our goal is to build tools for quantitative cell biology, using cryo-electron microscopy and tomography, cell biophysics, computational analysis, and integrative modeling. This potent combination allows us to look at macromolecular complexes in their native environment and derive their structure, context, and interaction partners.
Nuclear Periphery
Our current research is focused on studying the nuclear periphery, as nuclear biology remains one of the most exciting challenges in the cell, and it is uncharted territory structurally.

Our thrust in this area includes projects such as: the structural dynamics of the yeast nuclear pore complex, the mechanical communication between the cytoskeleton and the nucleus, and the molecular architecture of the genome and its association to the nuclear envelope.

We collaborate with different laboratories to open windows into various cellular events. These projects tend to have a translational component, and include studying the inner life of bacteria (with the labs of Kit Pogliano and Joe Pogliano), studying the effects of LRRK2 in Parkinson’s disease (with Susan Taylor), among others.