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Protein Structure Determination by Cryo-EM and X-Ray

Gunnar F. Schröder (Stuctural Biochemistry)

Most protein structures have been determined by X-ray crystallography and numerous new structures are added to the protein database every year. The technique allows to determine three-dimensional structures of materials at atomic-scale resolution provided that crystals are available. However, for proteins often crystallisation is challenging and may, in addition, distort the in-vivo structure of the protein. This applies in particular to transmembrane proteins and protein aggregates, such as fibres, for that crystal structures have often been lacking. Here, single-particle cryo-electron microscopy (cryo-EM) is increasingly used as a technique to determine the atomic structure of challenging biological systems. Recent advances in microscope engineering, electron detection, and image processing have allowed the structural determination of bigger and more flexible targets than possible with the complementary techniques X-ray crystallography and NMR spectroscopy. 

Wednesday, May 13, 15:00-16:30
Wednesday, May 27, 15:00-16:30

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