Electron Microscopy

  • A Space-Time Sensor for Light-Matter Interactions

    By using trains of extremely short electron pulses, LAP researchers have obtained time-resolved diffraction patterns from crystalline samples. In this image, patterns captured at attosecond intervals have been superimposed, thus revealing, in real time, the kind of electron motions that underlie atomic and subatomic phenomena. (Photo: Baum/Marimoto)

    Physicists in the Laboratory for Attosecond Physics (run jointly by LMU Munich and the Max Planck Institute for Quantum Optics) have developed an attosecond electron microscope that allows them to visualize the dispersion of light in time and space, and observe the motions of electrons in atoms. The most basic of all physical interactions in nature is that between light and matter. This interaction takes place in attosecond times (i.e. billionths of a billionth of a second). What exactly happens in such an astonishingly short time has so far remained largely inaccessible.

  • Less is more: Researchers develop a ‘molecular needle’ using a simplified biological system

    The type III secretion system (T3SS) is a needle-like molecular machine that gram negative bacteria use to infect cells. IMP-IMBA

    Minimalism is an increasingly popular lifestyle choice that encourages individuals to decrease the overall number of possessions owned and live more simply. According to minimalist philosophy, the reduction of unnecessary clutter enables one to live a more functional and purposeful existence. IMP-IMBA Group Leader and CSSB scientist Thomas Marlovits*, in collaboration with colleagues from Massachusetts Institute of Technology (MIT), discovered that a minimalist approach can also be applied to complex biological systems, such as the type III secretion system. The findings of this collaborative study have been published in the scientific journal, Nature Communications.

  • Lightwave Controlled Nanoscale Electron Acceleration Sets the Pace

    The waveform-controlled laser pulse creates a plasmon-enhanced near-field that drives the forward acceleration of an electron during its passage through the nanometer-sized metal cluster.  c University of Rostock

    Extremely short electron bunches are key to many new applications including ultrafast electron microscopy and table-top free-electron lasers. A german team of physicists from Rostock University, the Max Born Institute in Berlin, the Ludwig-Maxmilians-Universität Munich, and the Max Planck Institute of Quantum Optics in Garching has now shown how electrons can be accelerated in an extreme and well-controlled way with laser light, while crossing a silver particle of just a few nanometers.

  • Magnetization in Small Components can now be Filmed in the Laboratory

    Time-resolved measurement of the motion of a magnetic vortex core in the presence of an oscillating magnetic field. Ill./©: Daniel Schönke


    In the future, today's electronic storage technology may be superseded by devices based on tiny magnetic structures. These individual magnetic regions correspond to bits and need to be as small as possible and capable of rapid switching. In order to better understand the underlying physics and to optimize the components, various techniques can be used to visualize the magnetization behavior.

  • Mapping electromagnetic waveforms

    Mapping electromagnetic waveforms | A three-dimensional depiction of the spatial variation of the optical electromagnetic field around a microantenna following excitation with terahertz pulse. The optical field is mapped with the aid of electron pulses. Graphic: Dr. Peter Baum

    Munich Physicists have developed a novel electron microscope that can visualize electromagnetic fields oscillating at frequencies of billions of cycles per second. With this new microscope researchers will be able to obtain fundamental insights of how transistors or optoelectronic switches operate at the microscopic level.

  • Molecular structure of the cell nucleoskeleton revealed for the first time

    Nuclear lamina: architecture of delicate meshwork made of lamin filaments (filament rod in dark grey, globular domains in red) beneath nuclear membrane (transparent grey) and pore complexes (blue). Yagmur Turgay, University of Zurich

    Using 3D electron microscopy, structural biologists from the University of Zurich succeeded in elucidating the architecture of the lamina of the cell nucleus at molecular resolution for the first time. This scaffold stabilizes the cell nucleus in higher eukaryotes and is involved in organizing, activating and duplicating the genetic material. Diseases such as muscular dystrophy and premature aging, caused by mutations in the lamin gene, the major constituent of the lamina, can now be studied more effectively.

  • New Protein-sensing Mechanism Discovered

    Ribosome binding of NAC is mediated by a ribosome binding regulatory arm (N-αNAC, blue) and a translation sensor domain (N-βNAC, green). Martin Gamerdinger

    In a stunning discovery, molecular biologists from the University of Konstanz and ETH Zurich have been able to demonstrate that the nascent polypeptide-associated complex (NAC) senses newly synthesized proteins upon birth inside the ribosomal tunnel. New research published in Molecular Cell on 31 July 2019 conducted by researchers from the University of Konstanz’s Collaborative Research Centre 969 “Chemical and Biological Principles of Cellular Proteostasis” shows that the nascent polypeptide-associated complex (NAC) acts as a major protein identifying and, possibly, sorting device inside the cell.

  • Nonstop Tranport of Cargo in Nanomachines

    Cryo-electron microscopy reveals the structure of intraflagellar transport nanomachines (yellow, green) and the inhibitory mechanism of the dynein motor (blue). Jordan et al. Nature Cell Biology / MPI-CBG / Illustration: Bara Krautz


    Moving around, sensing the extracellular environment, and signaling to other cells are important for a cell to function properly. Responsible for those tasks are cilia, antenna-like structures protruding from most vertebrate cells. Whenever cilia fail to assemble correctly, their malfunctions can cause numerous human diseases. The assembly and maintenance of cilia requires a bidirectional transport machinery known as Intraflagellar Transport (IFT), which moves in train-like structures along the microtubular skeleton of the cilium.

  • Tailor-Made Membranes for the Environment

    Transmission electron microscope image of the membrane, provided by the Ernst Ruska-Centre. The two phases for proton and electron conduction are marked in colour. Forschungszentrum Jülich

    Jülich, 30 November 2016 – The combustion of fossil energy carriers in coal and gas power plants produces waste gases that are harmful to the environment. Jülich researchers are working on methods to not only reduce such gases, but also utilize them. They are developing ceramic membranes with which pure hydrogen can be separated from carbon dioxide and water vapour. The hydrogen can then be used as a clean energy carrier, for example in fuel cells. The researchers have now been able to increase the efficiency of these membranes to an unprecedented level. Their research results were published in Scientific Reports.

  • Watching Molecular Machines at Work

    Watching Molecular Machines at Work | Cryo EM structures of APC/C in three states: Left, off, before cells are ready for chromosome segregation; Middle, in the process of turning on; Right, on, in action, to turn on cell division. Illustration: Masaya Yamaguchi and Nicholas Brown, St. Jude Children’s Research Hospital

    An international team of scientists from Austria, Germany and the US has combined newly developed techniques in electron microscopy and protein assembly to elucidate how cells regulate one of the most important steps in cell division. The latest paper in a series of four is now published online in Molecular Cell.

  • World Record Resolution in Cryo-electron Microscopy

    Cryo-EM visualizes individual atoms in a protein for the first time. The cartoon shows a part of the apoferritin protein (yellow) with a tyrosine side chain highlighted in grey. Atoms are individually recognizable (red grid structures). © Holger Stark / Max Planck Institute for Biophysical Chemistry

    A crucial resolution barrier in cryo-electron microscopy has been broken. Holger Stark and his team at the Max Planck Institute (MPI) for Biophysical Chemistry have observed single atoms in a protein structure for the first time and taken the sharpest images ever with this method. Such unprecedented details are essential to understand how proteins perform their work in the living cell or cause diseases. The technique can in future also be used to develop active compounds for new drugs.