In 2014, Dubochet received EMBL's Lennart Philipson Award.[9] Describing his career in 2015, Professor Gareth Griffiths, his colleague at EMBL explained: "Jacques had a vision. He found a way of freezing thin films of water so fast that crystals had no time to form [that could damage samples] [...] over time the technique has become increasingly important to life science research, and it is clear today it is Nobel Prize-worthy."[3]
When asked by his university how he would like his Nobel Prize to be recognised by the institution he asked for a parking space for his bicycle which was duly given. He had cycled to his lab almost every day for 30 years.[15]
Dubochet is a member of the Social Democratic Party of Switzerland, and a member of the municipal parliament of Morges, where he holds a seat on the supervisory committee.[18][19] He is also part of the climate movement as a member of the Grandparents for Future and emphasized the urgency of saving our societies.[20]
Bibliography
(in French) Jacques Dubochet, Parcours, Éditions Rosso, 2018, 216 pages ( ISBN9782940560097).
↑ (in French) Muriel Raemy, "J'ai toujours voulu comprendre le monde", Moneta, journal of the Alternative Bank Switzerland, number 2 of year 2018, pages 21–22.
An electron microscope is a microscope that uses a beam of electrons as a source of illumination. They use electron optics that are analogous to the glass lenses of an optical light microscope to control the electron beam, for instance focusing them to produce magnified images or electron diffraction patterns. As the wavelength of an electron can be up to 100,000 times smaller than that of visible light, electron microscopes have a much higher resolution of about 0.1 nm, which compares to about 200 nm for light microscopes. Electron microscope may refer to:
Structural biology, as defined by the Journal of Structural Biology, deals with structural analysis of living material at every level of organization.
George Emil Palade was a Romanian-American cell biologist. Described as "the most influential cell biologist ever", in 1974 he was awarded the Nobel Prize in Physiology and Medicine along with Albert Claude and Christian de Duve. The prize was granted for his innovations in electron microscopy and cell fractionation which together laid the foundations of modern molecular cell biology, the most notable discovery being the ribosomes of the endoplasmic reticulum – which he first described in 1955.
Vitrification is the full or partial transformation of a substance into a glass, that is to say, a non-crystalline amorphous solid. Glasses differ from liquids structurally and glasses possess a higher degree of connectivity with the same Hausdorff dimensionality of bonds as crystals: dimH = 3. In the production of ceramics, vitrification is responsible for their impermeability to water.
The European Molecular Biology Laboratory (EMBL) is an intergovernmental organization dedicated to molecular biology research and is supported by 29 member states, two prospect member states, and one associate member state. EMBL was created in 1974 and is funded by public research money from its member states. Research at EMBL is conducted by more than 110 independent research groups and service teams covering the spectrum of molecular biology.
Carlos José Bustamante is a Peruvian-American scientist. He is a member of the National Academy of Sciences.
Transmission electron cryomicroscopy (CryoTEM), commonly known as cryo-EM, is a form of cryogenic electron microscopy, more specifically a type of transmission electron microscopy (TEM) where the sample is studied at cryogenic temperatures. Cryo-EM, specifically 3-dimensional electron microscopy (3DEM), is gaining popularity in structural biology.
Cryogenic electron tomography (cryoET) is an imaging technique used to reconstruct high-resolution (~1–4 nm) three-dimensional volumes of samples, often biological macromolecules and cells. cryoET is a specialized application of transmission electron cryomicroscopy (CryoTEM) in which samples are imaged as they are tilted, resulting in a series of 2D images that can be combined to produce a 3D reconstruction, similar to a CT scan of the human body. In contrast to other electron tomography techniques, samples are imaged under cryogenic conditions. For cellular material, the structure is immobilized in non-crystalline, vitreous ice, allowing them to be imaged without dehydration or chemical fixation, which would otherwise disrupt or distort biological structures.
Patrick Cramer is a German chemist, structural biologist, and molecular systems biologist. In 2020, he was honoured to be an international member of the National Academy of Sciences. He became president of the Max Planck Society in June 2023.
Martin Karplus is an Austrian and American theoretical chemist. He is the Director of the Biophysical Chemistry Laboratory, a joint laboratory between the French National Center for Scientific Research and the University of Strasbourg, France. He is also the Theodore William Richards Professor of Chemistry, emeritus at Harvard University. Karplus received the 2013 Nobel Prize in Chemistry, together with Michael Levitt and Arieh Warshel, for "the development of multiscale models for complex chemical systems".
The Max Planck Institute of Biophysics is located in Frankfurt, Germany. It was founded as the Kaiser Wilhelm Institute of Biophysics in 1937, and moved into a new building in 2003. It is an institute of the Max Planck Society.
Richard Henderson is a British molecular biologist and biophysicist and pioneer in the field of electron microscopy of biological molecules. Henderson shared the Nobel Prize in Chemistry in 2017 with Jacques Dubochet and Joachim Frank. "Thanks to his work, we can look at individual atoms of living nature, thanks to cryo-electron microscopes we can see details without destroying samples, and for this he won the Nobel Prize in Chemistry."
Stefan Walter Hell is a Romanian-German physicist and one of the directors of the Max Planck Institute for Multidisciplinary Sciences in Göttingen, and of the Max Planck Institute for Medical Research in Heidelberg, both of which are in Germany. He received the Nobel Prize in Chemistry in 2014 "for the development of super-resolved fluorescence microscopy", together with Eric Betzig and William Moerner.
Cryofixation is a technique for fixation or stabilisation of biological materials as the first step in specimen preparation for the electron microscopy and cryo-electron microscopy. Typical specimens for cryofixation include small samples of plant or animal tissue, cell suspensions of microorganisms or cultured cells, suspensions of viruses or virus capsids and samples of purified macromolecules, especially proteins.
In molecular biology, the term macromolecular assembly (MA) refers to massive chemical structures such as viruses and non-biologic nanoparticles, cellular organelles and membranes and ribosomes, etc. that are complex mixtures of polypeptide, polynucleotide, polysaccharide or other polymeric macromolecules. They are generally of more than one of these types, and the mixtures are defined spatially, and with regard to their underlying chemical composition and structure. Macromolecules are found in living and nonliving things, and are composed of many hundreds or thousands of atoms held together by covalent bonds; they are often characterized by repeating units. Assemblies of these can likewise be biologic or non-biologic, though the MA term is more commonly applied in biology, and the term supramolecular assembly is more often applied in non-biologic contexts. MAs of macromolecules are held in their defined forms by non-covalent intermolecular interactions, and can be in either non-repeating structures, or in repeating linear, circular, spiral, or other patterns. The process by which MAs are formed has been termed molecular self-assembly, a term especially applied in non-biologic contexts. A wide variety of physical/biophysical, chemical/biochemical, and computational methods exist for the study of MA; given the scale of MAs, efforts to elaborate their composition and structure and discern mechanisms underlying their functions are at the forefront of modern structure science.
Henning Stahlberg is a German physicist and Professor at the Swiss Federal Institute of Technology Lausanne and the University of Lausanne, Switzerland.
Joachim Frank ; born September 12, 1940) is a German-American biophysicist at Columbia University and a Nobel laureate. He is regarded as the founder of single-particle cryo-electron microscopy (cryo-EM), for which he shared the Nobel Prize in Chemistry in 2017 with Jacques Dubochet and Richard Henderson. He also made significant contributions to structure and function of the ribosome from bacteria and eukaryotes.
Cryogenic electron microscopy (cryo-EM) is a cryomicroscopy technique applied on samples cooled to cryogenic temperatures. For biological specimens, the structure is preserved by embedding in an environment of vitreous ice. An aqueous sample solution is applied to a grid-mesh and plunge-frozen in liquid ethane or a mixture of liquid ethane and propane. While development of the technique began in the 1970s, recent advances in detector technology and software algorithms have allowed for the determination of biomolecular structures at near-atomic resolution. This has attracted wide attention to the approach as an alternative to X-ray crystallography or NMR spectroscopy for macromolecular structure determination without the need for crystallization.
Cryomicroscopy is a technique in which a microscope is equipped in such a fashion that the object intended to be inspected can be cooled to below room temperature. Technically, cryomicroscopy implies compatibility between a cryostat and a microscope. Most cryostats make use of a cryogenic fluid such as liquid helium or liquid nitrogen. There exists two common motivations for performing a cryomicroscopy. One is to improve upon the process of performing a standard microscopy. Cryogenic electron microscopy, for example, enables the studying of proteins with limited radiation damage. In this case, the protein structure may not change with temperature, but the cryogenic environment enables the improvement of the electron microscopy process. Another motivation for performing a cryomicroscopy is to apply the microscopy to a low-temperature phenomenon. A scanning tunnelling microscopy under a cryogenic environment, for example, allows for the studying of superconductivity, which does not exist at room temperature.
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