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.
The 26S proteasome is 2.6 MDa multisubunits protease responsible for the regulated degradation of polyubiquitylated proteins. To understand how the 26S proteasome executes its function, we take a multidisciplinary approach combining cryo-EM single particle analysis with biochemical and computational studies.
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.