Press Releases of the Baumeister Department

Wolfgang Baumeister wins Stifterverbandspreis 2019
The biophysicist has revolutionized molecular structural biology with the help of cryo-electron tomography. [more]
Crowd Control

Crowd Control

July 02, 2018
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]
<p style="text-align: left;" align="center">Ernst Jung Prize awarded to Wolfgang Baumeister</p>
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]
<p style="text-align: left;" align="center">Decoding the structure of the huntingtin protein</p>
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]
Guardians of the Gate

Guardians of the Gate

December 11, 2017
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]
<p style="text-align: left;" align="center"><strong>Weeds in the brain</strong></p>

Weeds in the brain

September 07, 2017
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 battery compartments of the 26S Protein Recycling Machine
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]
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