Alzheimer’s and Parkinson’s diseases and other neurodegenerative diseases are associated with protein aggregations that arise when proteins misfold and clump into larger, often insoluble structures.

We study the macromolecular basis of how proteins and lipids interact during aggregation: What is their architecture? What precursors do they require? What sub-cellular environment supports them?

What sets our work apart is that we study protein aggregation in situ, which can reveal what these aggregates look like and how they behave in their natural cellular environment.

We developed a neuronal co-culture cryo-platform uniquely compatible for specialized cryo-fixation that preserves cells in a “glassy” state without chemical fixatives and without ice crystals that destroy tissues and cells. This enables correlative light and electron microscopy (CLEM) of near-native neuronal networks.

We harness cellular structural biology techniques and complementary methods. We also develop and apply new interfaces and technologies for cryo-focused ion beam milling (cryo-FIB) and cryo-electron tomography (cryo-ET).

These tools, combined with advanced computation, allows to view nanoscale details inside a cell preserved in a near-native state, either healthy or diseased.