Henning Stahlberg | |
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 Henning Stahlberg (2011) | |
| Born | Nov. 18, 1965 Berlin |
| Nationality | German and Swiss |
| Scientific career | |
| Fields | Physicist |
| Institutions | Technische Universität Berlin, University of California, Davis, Biozentrum University of Basel, École Polytechnique Fédérale de Lausanne |
Henning Stahlberg is a German physicist and Professor at the Swiss Federal Institute of Technology Lausanne and the University of Lausanne, Switzerland.
Henning Stahlberg studied physics at the Technische Universität Berlin and graduated with a doctorate from the Swiss Federal Institute of Technology in Lausanne (EPFL) in 1997. He continued his research as a postdoctoral fellow at the Biozentrum, University of Basel for the following 6 years. From 2003 he joined the University of California in Davis as assistant professor, where he was promoted to tenured associate professor in 2007. From 2009 to 2020, Stahlberg was a Full Professor for Structural Biology at the Biozentrum of the University of Basel, where he headed the Center for Cellular Imaging and NanoAnalytics (C-CINA). [1] Since 2020, Stahlberg holds a dual-affiliation as a Full Professor for Physics at the Institute of Physics of the Basic Sciences division of the EPFL and as a Full Professor in the Faculty of Biology and Medicine of the University of Lausanne, Switzerland. He heads the Laboratory of Biological Microscopy at the EPFL and is establishing the Dubochet Center for Imaging in Lausanne. [2]
Henning Stahlberg studies biological membrane systems from the atomic structure of individual proteins to the cellular context of the system. Employing cryo-electron microscopy, electron tomography, and correlative light and electron microscopy CLEM, he investigates the structure of ion channels [3] and membrane transporters, [4] and studies the molecular and cellular events in Parkinson's disease. [5] Further, he develops computational algorithms for the 3D reconstruction of proteins. Using these methods, Stahlberg successfully elucidated among other things the 3D structure of the Type III Secretion System (T3SS) in intact bacteria. [6] He developed the 2dx software to reconstruct the 3D structure of membrane proteins from cryo-electron microscopy images of 2D crystals, which the group merged into the FOCUS software for online data processing of cryo-EM data. [7] [8] [9]
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.
The Max Planck Institute of Biochemistry is a research institute of the Max Planck Society located in Martinsried, a suburb of Munich. The institute was founded in 1973 by the merger of three formerly independent institutes: the Max Planck Institute of Biochemistry, the Max Planck Institute of Protein and Leather Research, and the Max Planck Institute of Cell Chemistry.
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.
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."
Eva Nogales is a Spanish-American biophysicist at the Lawrence Berkeley National Laboratory and a professor at the University of California, Berkeley, where she served as head of the Division of Biochemistry, Biophysics and Structural Biology of the Department of Molecular and Cell Biology (2015–2020). She is a Howard Hughes Medical Institute investigator.
Single particle analysis is a group of related computerized image processing techniques used to analyze images from transmission electron microscopy (TEM). These methods were developed to improve and extend the information obtainable from TEM images of particulate samples, typically proteins or other large biological entities such as viruses. Individual images of stained or unstained particles are very noisy, and so hard to interpret. Combining several digitized images of similar particles together gives an image with stronger and more easily interpretable features. An extension of this technique uses single particle methods to build up a three-dimensional reconstruction of the particle. Using cryo-electron microscopy it has become possible to generate reconstructions with sub-nanometer resolution and near-atomic resolution first in the case of highly symmetric viruses, and now in smaller, asymmetric proteins as well. Single particle analysis can also be performed by inductively coupled plasma mass spectrometry (ICP-MS).
Crystallographic image processing (CIP) is traditionally understood as being a set of key steps in the determination of the atomic structure of crystalline matter from high-resolution electron microscopy (HREM) images obtained in a transmission electron microscope (TEM) that is run in the parallel illumination mode. The term was created in the research group of Sven Hovmöller at Stockholm University during the early 1980s and became rapidly a label for the "3D crystal structure from 2D transmission/projection images" approach. Since the late 1990s, analogous and complementary image processing techniques that are directed towards the achieving of goals with are either complementary or entirely beyond the scope of the original inception of CIP have been developed independently by members of the computational symmetry/geometry, scanning transmission electron microscopy, scanning probe microscopy communities, and applied crystallography communities.
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.
Ueli Aebi is a Swiss structural biologist and co-founder of the Maurice E. Müller Institute for Structural Biology at the Biozentrum University of Basel.
Andreas Engel is a Swiss structural biologist and co-founder of the Maurice E. Müller Institute for Structural Biology at the Biozentrum of the University of Basel.
Chikashi Toyoshima (豊島 近, Toyoshima Chikashi, born July 17, 1954) is a Japanese biophysicist. His research focuses on two proteins: the Ca2+-ATPase of muscle sarcoplasmic reticulum, and the Na+, K+-ATPase expressed in all animal cells. He is a professor at the University of Tokyo and the Foreign Associate of the National Academy of Sciences, USA. Toyoshima's research about the Ca2+-ATPase started in 1989, and within a few years of beginning this research, he and his colleagues obtained the world's first series of images of Ca2+-ATPase at the atomic level. Via x-ray crystallography, cryo-EM and other methods, he has determined the crystal structures of ten intermediates of Ca2+-ATPase. On September 10, 2015, The Royal Swedish Academy of Sciences awarded him and Poul Nissen the Gregori Aminoff Prize of 2016 for their fundamental contributions to understanding the structural basis for ATP-driven translocation of ions across membranes.
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.
Jacques Dubochet is a retired Swiss biophysicist. He is a former researcher at the European Molecular Biology Laboratory in Heidelberg, Germany, and an honorary professor of biophysics at the University of Lausanne in Switzerland.
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.
Tamir Gonen is an American structural biochemist and membrane biophysicist best known for his contributions to structural biology of membrane proteins, membrane biochemistry and electron cryo-microscopy (cryoEM) particularly in electron crystallography of 2D crystals and for the development of 3D electron crystallography from microscopic crystals known as MicroED. Gonen is an Investigator of the Howard Hughes Medical Institute, a professor at the University of California, Los Angeles, the founding director of the MicroED Imaging Center at UCLA and a Member of the Royal Society of New Zealand.
Suliana Manley is an American biophysicist. Her research focuses on the development of high-resolution optical instruments, and their application in studying the organization and dynamics of proteins. She is a professor at École Polytechnique Fédérale de Lausanne and heads the Laboratory of Experimental Biophysics.
Giulia Zanetti is a British Italian biologist and Professor of Molecular Biology at the Francis Crick Institute. She develops advanced imaging techniques to understand membrane transport pathways. She was awarded the 2021 Biochemical Society Colworth Medal.
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