The biophysicist has revolutionized molecular structural biology with the help of cryo-electron tomography. [more]

Have you ever been stuck in the middle of a crowd? As people pack closer together, it becomes more difficult to move through the crowd. Sometimes it can become so tightly packed that you cannot move at all. If this sounds uncomfortable, then you probably wouldn’t like to live inside a cell, which is densely packed with proteins and other molecules. This crowding is very important for the cell—it pushes the molecules together so that they can interact and perform the chemical reactions that the cell needs to live. In fact, many human diseases are likely influenced by changes in molecular crowding that cause harmful interactions between proteins. Despite its importance, it remains a mystery how the crowding inside cells is controlled. Combining biophysics, cell biology, physical modeling, and cryo-electron tomography, an international team of scientists at New York University (NYU) and the Max Plank Institute of Biochemistry (MPIB) has discovered that the mTORC1 signaling pathway controls the concentration of ribosomes inside the cell, thereby regulating crowding and the ability of proteins to interact with each other to form phase-separated compartments. This study is published in the journal Cell. [more]

The Ernst Jung Gold Medal for Medicine is awarded for lifetime achievement by a scientist who has made a major contribution to the advancement of medicine. This year’s prize was awarded to Munich biophysicist Wolfgang Baumeister for his work in the field of cryo-electron microscopy and in elucidating the structure of large macromolecular protein complexes. Wolfgang Baumeister is Director at the Max Planck Institute of Biochemistry in Martinsried. The prize includes a €30,000 scholarship for Baumeister to award to a junior scientist of his choice. The prize was awarded at a ceremony in Hamburg on 4 May 2018. [more]

25 years ago, the cause of Huntington's disease was discovered. Mutations on a single gene, the huntingtin gene, lead to an incorrect form of the correspondent protein. With the help of cryo-electron microscopy, the recently awarded Nobel Prize winning method, researchers have now decoded the three-dimensional, molecular structure of the healthy human huntingtin protein. This now enables its functional analysis. An improved understanding of the structure and the function of the huntingtin protein could contribute to the development of new treatment methods in the future. The work of the researchers from the Max Planck Institute of Biochemistry in Martinsried and Ulm University has now been published in the journal Nature. [more]

To travel between the cytoplasm and the nucleus, proteins must pass through a gateway called the nuclear pore complex (NPC). However, it is unknown whether the cell can monitor the proteins that go through the NPC. Using in situ cryo-electron tomography to look into cells that are frozen in a life-like state, scientists at the Max Planck Institute of Biochemistry discovered that NPCs are decorated with highly organized clusters of proteasomes, molecular machines that destroy misfolded and mislocalized proteins to ensure healthy cell function. These NPC-tethered proteasomes may perform surveillance of NPC trafficking to ensure that only the correct proteins pass into, or out of, the nucleus. The study is published in the journal PNAS. [more]

A common feature of neurodegenerative diseases such as Alzheimer’s, Parkinson’s, and Huntington’s is the accumulation of toxic protein deposits in the nerve cells of patients. Once these aggregates appear, they begin to proliferate like weeds. If and how these deposits damage nerve cells and lead to their demise remains largely unexplained. A detailed insight into the three-dimensional structure of the protein aggregates should help researchers to solve this puzzle. Now, using cryo-electron tomography, scientists at the Max Planck Institute of Biochemistry in Martinsried near Munich have succeeded in generating a high-resolution, three-dimensional model of the huntingtin aggregates responsible for Huntington’s disease. The results are published in the journal Cell.   [more]

The degradation of proteins and the re-use of their basic building blocks is a process that is a matter of survival in cells. Researchers at the Max-Planck-Institute for Biochemistry present a detailed structure of the human protein recycling machine, the so-called 26S proteasome, in near-atomic resolution in their latest article published in PNAS. The high-resolution structure enabled the scientists to visualize the molecular energy carriers bound to the 26S proteasome, which provide the power for proteasome function. Detailed knowledge of the exact structure is the basis for the development of drugs for the treatment of cancers and neurodegenerative diseases. [more]

Using a combination of the latest technological developments in the area of cryo-electron tomography, scientists from the Max Planck Institute of Biochemistry in Martinsried captured three-dimensional images of previously concealed structures in and around the nucleus of HeLa cells. They now present for the first time images of the nuclear lamina, a nanometer-thin filamentous protein structure that supports the nucleus, in the journal Science. The cellular components are observed in their natural environment without the cells being chemically altered or dehydrated. This is the only approach that allows visualization and understanding of the interactions between different functional components of a cell. [more]

The Golgi apparatus serves as a cellular post office, sending the cell’s many proteins to their correct destinations. In order to mark and sort the proteins, the Golgi has an elaborate architecture. It consists of flat membrane-enclosed compartments (called cisternae) that are densely packed on top of each other, like a stack of pancakes. Researchers at the Max Planck Institute (MPI) of Biochemistry in Martinsried near Munich, Germany, have now identified structures within these cisternae. “Using cryo-electron tomography, we discovered that the cisterna membranes are held together by linker proteins,” explains Benjamin Engel, first author of the study. [more]

Neurodegenerative diseases like Alzheimer’s, Huntington’s or Parkinson’s are caused by defect and aggregated proteins accumulating in brain nerve cells that are thereby paralyzed or even killed. In healthy cells this process is prevented by an enzyme complex known as the proteasome, which removes and recycles obsolete and defective proteins. Recently, researchers in the team of Wolfgang Baumeister at the Max Planck Institute of Biochemistry in Martinsried near Munich were the first to observe and structurally characterize proteasomes at work inside healthy brain cells. “When we saw the proteasomes on our screen, we were immediately aware of the major importance of the results”, remembers Shoh Asano, first author of the study. The study has now been published in the journal Science. [more]

Photosynthesis sustains most of the life on our planet. It harvests energy from sunlight, while generating oxygen and removing carbon dioxide from the atmosphere. The process takes place in the chloroplasts of plants and algae. Researchers in the team of Wolfgang Baumeister at the Max Planck Institute of Biochemistry in Martinsried near Munich were recently successful in revealing the native structure of the chloroplast in 3D. “The results are the first of their kind and provide us with new insights into the mechanisms of photosynthesis”, says Benjamin Engel, first author of the study. The results were recently published in the journal eLife. [more]

Neurodegenerative diseases such as Alzheimer's, Parkinson's, Huntington's disease and amyotrophic lateral sclerosis (ALS) are characterized by toxic protein aggregates in certain regions of the brain and nerve cells. The objective of the project of F.-Ulrich Hartl, Wolfgang Baumeister, Rüdiger Klein and Matthias Mann is to elucidate just how this aggregation process is linked to cytotoxicity and cell death. For their project, the four directors of the Max Planck Institutes of Biochemistry and of Neurobiology in Martinsried near Munich, Germany, have now been awarded a Synergy Grant of the European Research Council (ERC). The four professors will use the 13.9 million euros in funding to establish closely collaborating research groups throughout the project lifetime of six years. The ERC Synergy Grant is the most highly endowed research grant of the European Union and was awarded this year for the first time [more]

Uncontrolled or inaccurate degradation of cellular proteins can lead to diseases like cancer or Alzheimer’s disease. Scientists of the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich, Germany, have now uncovered the structure and the operating mechanism of an important component of the human cellular degradation machinery, tripeptidyl peptidase II (TPPII). “Decoding the structure of TPPII is a crucial milestone towards understanding the complex activation and control of protein degradation”, says Beate Rockel, scientist at the MPIB. The results of the study have now been published in the journal Structure. [more]

Cryo-electron tomography provides high-resolution, three-dimensional insights into the cell. However, with this method only very small cells or thin peripheral regions of larger cells can be investigated directly. Scientists of the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich have now developed a procedure to provide access to cellular regions which were previously nearly inaccessible. Using focused ion beam (FIB) technology, specific cellular material can be cut out, opening up thin “windows” into the cell’s interior. This alternative approach enables the preparation of larger cellular samples devoid of artefacts. Then the samples can be analyzed in high resolution using electron tomography. The study of the MPIB scientists was recently published in the Proceedings of the National Academy of Sciences USA. [more]

It’s the small things that matter in life. In structural biology these include proteins, enzymes and viruses. A single change in their molecular structure can mean the difference between function and malfunction, health and disease. The three-dimensional shape of a molecule such as a protein helps scientists to understand how it functions and its impact on the cell and the organism. On Thursday, February 23, the EU project ‘Instruct’ launches a new distributed research infrastructure for the science of structural biology. The launch of Instruct will give academic and commercial scientists across Europe access to a full portfolio of integrated technologies. Wolfgang Baumeister, director at the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich, Germany, is one of the members of the Instruct consortium [more]

Defective proteins that are not disposed of by the body can cause diseases such as Alzheimer’s or Parkinson’s. Scientists at the Max Planck Institute (MPI) of Biochemistry recently succeeded in elucidating the structure of the cellular protein degradation machinery (26S proteasome) by combining different methods of structural biology. The results of a collaboration with colleagues from the University of California, San Francisco and the Swiss Federal Institute of Technology Zurich (ETH Zürich) represent an important step forward in the investigation of the 26S proteasome. The findings have now been published in Proceedings of the National Academy of Sciences PNAS. [more]

Due to cell-biological research, it is already known which components of the cell are responsible for the production of proteins. But so far it has not been explored in detail how these protein factories (ribosomes) are organized inside the cell. Recently, scientists at the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich, Germany, succeeded in mapping the inner life of an intact human cell three-dimensionally via cryo-electron tomography. In this way they were able to show where the ribosomes are located in the cell and how they are arranged. In the past, this was only possible with bacterial cells. The results have now been published in Molecular Cell. [more]

The human brain consists of more than 100 billion nerve cells, and each of them is able to communicate with thousands of its neighbors. Nerve signals let us move, act and think. Scientists of the Max Planck Institute (MPI) of Biochemistry in Martinsried near Munich have now succeeded in obtaining detailed 3D images of synapses, the connections where communication between nerve cells takes place. “With the help of cryoelectron tomography, we could detect and analyze structures in synapses that no one else could see before,” says Rubén Fernández-Busnadiego, scientist at the MPI of Biochemistry. The work has now been published as the cover story in the Journal of Cell Biology. [more]

Each cell in an organism possesses its own protein factories known as ribosomes. Every second, these enzyme complexes produce new proteins with messenger molecules (mRNA) from the cell nucleus as blueprints. In order to generate as many proteins as possible at the same time, several ribosomes cluster together to form an “industrial complex” – the polysome - and read simultaneously the same messenger molecule. Scientists at the Max-Planck-Institute of Biochemistry have now, for the first time, been able to reveal the three-dimensional structure of these complexes (Cell, January 23, 2009). [more]

The first 3-D images that disclosure a double membrane surrounding mycobacteria were recorded by Martinsried scientists, ending a long scientific debate about the mycobacterial outer membrane and opening new pathways to improve the development of chemotherapeutic substances against tuberculosis (PNAS March 11th, 2008). [more]

Unique "near-field" microscopy at the MPI of Biochemistry (Martinsried near Munich) allowed, for the first time, viewing on the nanoscale the spontaneous appearance and growth of metallic puddles that mark the transition from an electrically insulating material ino an electrically conducting one. [more]

It is not only migratory birds that orient themselves to the magnetic field of the Earth. Also bacteria - supposedly "simple" organisms - have evolved to be able to take advantage of the magnetic field in their search for optimal living conditions. Such "magnetotactic"microorganisms use a miniature, cellular compass made of a chain of single nanomagnets, called magnetosomes. The entire bacterium is oriented like a compass needle inside the magnetic field. Until now, it was not clear how the cells organise magnetosomes into a stable chain, against their physical tendency to collapse by magnetic attraction. But using modern molecular-genetic and imaging processes, researchers from the Max Planck Institue for Marine Microbiology in Bremen and Max Planck Institute of Biochemistry in Martinsried, Germany have identified the protein responsible for creating the magnetosome chain. The scientists showed that this protein aligns the magnetosomes along a cytoskeletal structure which was previously unknown. This points to evidence that genetics regulate the magnetosome chain exactly. The structure is one of the most complex that has ever been found in bacterial cells. It is comparable to organelles that, until now, scientists had only been familiar with in higher organisms. (Nature, Advanced Online Publication, November 20, 2005). [more]

Wolfgang Baumeister is famous for his work on proteasome and the further development of electron tomography. So, he provides high-definition, three-dimensional pictures of intact cells and could gain insights in their supramolecular structures. For this, he has now been honored with the Louis-Jeantet-Prize for Medicine 2003. [more]