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Nobel prize for cryo-Electron Microscopy


Jacques Dubochet, Joachim Frank and Richard Henderson have been awarded the 2017 Nobel prize for Chemistry “for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution" a method by which the structure of biological matter can be analysed at the atomic scale.

In the 1980s Jacques Dubochet and his group at the EMBL in Heidelberg, and later on at the University of Lausanne, found a way to vitrify thin electron-lucent layers of water and aqueous solutions. It then became possible to image biological matter flash-frozen within its native environment. In parallel, Joachim Frank, at Albany then Columbia University, laid the ground of the numerical tools to reconstruct the 3D structure of macromolecules from 2D cryo-electron microscopy images. Richard Henderson pioneered electron crystallography of protein 2D-crystals and played a major role in the development of the last generation of electron detectors, essential players of the recent Cryo-electron microscopy “resolution revolution”.

Cryo-electron microscopy is no less important in the field of soft matter physics. It has been installed at the LPS as early as the mid 1990s, by Françoise Livolant and Amélie Leforestier, back from post-doc in Dubochet’s group. A collaboration ensues based on the two teams long-lasting interest on DNA and chromosomes.

Cryo-electron microscopy is now widely used in the “soft matter and physics-biology interface” pole, with applications in the fields of polymer and polyelectrolytes, liquid crystals, nanomaterials or physical virology.

Cryo-electron microscopy at the LPS. (A) Cubosome (phytantriol/polymer/water). (B) S Superlattices of Gold Nanoparticles. (C) Phage capsid containing DNA collapsed in a toroidal form. (D) Crystalline liquid phase of nucleosomes. Scale bar : 20 nm.

Image references
(A) Latypova L, Gozdz WT, Pieranski P (2014) Facets of lyotropic liquid crystals Langmuir 30(2), 488-95.
(B) Schmitt J, Hajiw S, Lecchi A, Degrouard J, Salonen A, Impéror-Clerc M, Pansu B. (2016) Formation of Superlattices of Gold Nanoparticles Using Ostwald Ripening in Emulsions : Transition from fcc to bcc Structure. J Phys Chem B. 120, 5759-66.
(C) Leforestier A, Livolant F (2009) Structure of toroidal DNA collapse inside the phage capsid. Proc. Natl. Acad. Sci. USA 106, 9157-9162.
(D) Leforestier A, Dubochet J, Livolant F (2001) Bilayers of nucleosome core particles. Biophys. J. 81, 2414-2421.

Voir en ligne : Website of the Nobel Prize in Chemistry