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MICROSCOPY & IMAGING


Dr Alistair Siebert from eBIC And Alex Buzduga (ThermoFisher) operate Krios 1


THE FUTURE OF


he development of cryo-electron microscopy (cryo-EM) allowed a leap forward in imaging the structure and function of individual biological molecules, an achievement rewarded with a Nobel prize in 2017. Now cryo-electron tomography (cryo-ET) is emerging as a powerful method for performing structural studies in unperturbed environments, i.e. in situ. Tis offers the potential to study functional modules and their interactions, the molecular sociology of cells, with near-atomic resolution.


IMAGING? T


Emma Doughty discusses the potential, and challenges, of cryo-electron tomography


TECHNICAL DEVELOPMENTS IN STRUCTURAL BIOLOGY X-ray crystallography used to be the pre-eminent method for imaging biomolecular structures. Tis workhorse of the bioimaging world has led to countless discoveries, and will continue to do so. However, X-ray crystallography has a serious limitation – it can only be used to investigate crystallised proteins. Researchers can spend years trying to coax uncooperative proteins into crystals suitable for analysis, and some of the most biologically important molecules are still resisting their attempts. Furthermore,


for more complicated biomolecules it becomes increasingly difficult to make useful crystals. In the early 1980s, Jacques Dubochet


developed a technique to ‘vitrify’ molecules by flash-freezing solutions of proteins using liquid ethane, which prevents water-soluble biomolecules from drying out in a vacuum, allows them to retain their natural shape, and keeps them relatively still during electron microscopy, and cryo-EM was born. Since then, improvements in the sensitivity of electron microscopes, in sample preparation techniques and


www.scientistlive.com 57


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