Cryo-Electron Tomography (CET) is used for the study of the supramolecular architecture of frozen hydrated cells in three dimensions at nanometer resolution. CET is based on the principle of any 'tomographic' technique: the acquisition of images from different viewing angles of a three dimensional object and the subsequent reconstruction of that particular structure.

This project explores the mostly uncharted area of alternative phase contrast methods for TEM. In particular, the development and applications of thin film phase plates and the associated hardware and software.

We study the structural mechanisms by which protein aggregation can be toxic to cells, leading to neurodegenerative diseases such as Alzheimer’s or Parkinson’s.

We are interested in the molecular organization of actin structures in their native environment, and how it enables actin filaments to exert or resist against forces.

We use cryo-electron tomography to map the organization of macromolecules within native organelles, with the aim of understanding how organelle architecture orchestrates molecular function.

Synapses are functional connection points between neurons, transmitting a presynaptic electrical signal (action potential) to the postsynaptic neuron. We use cryo-electron tomography to reveal the architecture of complexes involved in synaptic transmission and to obtain more information about their function.