Cryo Electron Tomography
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.
Visual Proteomics
By help of the cryo-EM technique described above we are able to do molecular mapping of whole cells. This can tells us, where different proteins are located, and even when and where new proteins are built up and others are degraded.
Vitreous Cryosectioning
In this challenging technique, rapidly frozen (vitreous) cells or small pieces of tissue are cut into thin slices for subsequent structural investigation by cryo- light and electron microscopy.
20S Proteasome
This protein is the proteolytic core complex of the 26S proteasome (see next section). It consists of 4 rings built of two different types of subunits, its architecture is conserved from archae to humans.
26S Proteasome
This multi-subunit complex consists of the 20S core and two 19S cap proteins. Its function in the cell is to degrade ubiquitinated substrates in an ATP-dependent manner.
Tripeptidyl Peptidase II
This serine protease of the subtilisin type consists of 150 KDa monomers, which assemble into a 6 MDa complex. Its biological functions are degradation of oligopeptides into tripeptides, it is implicated in muscle sepsis and apoptosis, trimming of antigenic peptides and degradation of neuropeptides
70S Ribosome
This ribonucleoprotein particle (ca. 2.7 MDa) is responsible for translation, the expression of the genetic code from mRNA into protein. Its activity depends on the interaction with many other macromolecules and it is highly regulated.
Membrane and Cell Wall Proteins
The cell envelope of bacteria and archaea contains proteins for transport or translocation of ions, nutrients and macromolecules as well as proteins supporting the structural integrity of the cell. Porins of the bacterial outer membrane, the structure of the mycobacterial outer membrane, and surface proteins from archaea and bacteria are in the focus of our projects.
Modeling of Protein Complexes
Complexes that are associated to lipid membranes carry out many important cellular functions, but their structures are largely elusive to date. We unravel the structures of membrane-associated complexes by integration of cryoelectron tomographic data into modeling of protein assemblies.
Molecular Architecture of Synaptic Complexes
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.
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