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Liquid phase electron microscopy (LPEM) offers remarkable capabilities with regards to imaging label-free, time resolved-structures in liquid by removing the artefacts caused by traditional drying or cryogenic treatments. One of the most attractive applications of LPEM is the investigation of cell molecular machinery structures such as proteins. The liquid nature of the sample presents novel opportunities such as accessing previously inaccessible protein states or the possibility of 3D structure reconstruction by applying tomographic methods.
During this Nanotalk, Dr. Ruiz-Pérez presents research on the combination of all-atom simulations with LPEM to complement protein structural studies with dynamic investigations. She reveals how she was able to exploit LPEM and our Stream system to image the dynamics of proteins undergoing Brownian motion. Via tomographic techniques, she shows how to utilize the proteins' natural rotation to access the particle structural landscape for reconstructing its architecture in 3D.
The use of LTEM for the investigation of proteins is not limited to 3D reconstruction and structural analysis. Dr. Ruiz-Pérez and her collaborators have employed LPEM to image and screen amyloid-β (Aβ) aggregation. Aβ is a small, disordered peptide with 36-43 amino acids. Aβ accumulates into stages of microscopic amyloid fibres and plaques that are found in brains affected by Alzheimer’s disease (AD). Preliminary investigations on Aβ aggregation, via LTEM are presented during this Nanotalk. This work, although still in early stages, promises to provide relevant and novel biological information on Aβ aggregation pathways.
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