Nobel prize 2017 for cryo-electron microscopy

5 October 2017
​The Nobel prize for Chemistry 2017 went to 3 investigators (Jacques Dubochet, Joachim Frank and Richard Henderson) whose scientific contributions have led to our current ability to determine the 3D-structure of biomolecules by cryo-electron microscopy. 

Conventional preparation techniques for electron microscopy use chemical preparation of biological samples, inevitably influencing the observed ultrastructure to a more or lesser extent.  Cryo-EM at the other hand, uses ultra-rapid cooling of a very thin film of a suspension containing the molecules of interest, vitrifying the sample without formation of ice-crystals that could damage the ultrastructure.  By applying mathematical algorithms (single particle analysis) to thousands of images of the molecules of interest in many different orientations in the vitrified suspension, the 3D-structure of the molecules is revealed. By recent technological advances in instrumentation it is now possible to obtain 3D-structures at atomic resolution.  This information can contribute to solving many questions in biomedical context.  See also www.Nobelprize.org.

Expertise in the VIB centers
The VIB Electron Microscopy Platform in Leuven under guidance of Natalia Gunko in the VIB-KU Leuven Center for Brain & Disease uses cryo-EM for elucidating ultrastructural features of lipid structures in particular (exosomes, liposomes, etc.) with less demanding resolution requirements. The Rouslan Efremov lab at the VIB-VUB Center for Structural Biology a high-end cryo-electron microscope (expected 2018) for pursuing 3D-structure of biomolecules as described above.