Dr. Max Ruwolt
Structural mass spectrometry support for the Freund Lab.
Biochemistry
Postdoc - Mass Spectrometry
63
Room 031
14195 Berlin
In his role as a postdoctoral researcher, Max supports ongoing projects on SNARE and MHC complexes and contributes to the broader research of TRR186, which aims to investigate various molecular switches. With his strong expertise in structural mass spectrometry, with a focus on cross-linking mass spectrometry, he complements established structural techniques at the Freund Lab, such as NMR and cryo-EM. During his postdoc, he seeks to develop further methods for detecting post-translational modifications that function as key molecular switches.
In addition, he will use proximity labeling to identify mechanistically relevant protein-protein interactions. Lastly, his interests also include establishing immunopeptidomics and chemoproteomics pipelines that can support a wide range of projects across different research groups.
Ever since my first experiences in biochemistry, I have been motivated to learn powerful technologies that enable discovery-driven research. During my bachelor’s at Freie Universität Berlin and the Robert Koch Institute, I used proximity labelling to investigate the entry mechanism of pathogenic Chlamydia into host cells. In my master’s at Freie Universität Berlin, I explored X-ray crystallography, virology, and glycobiology. Building on this background in bioanalytics and structural biology, I pursued a PhD in Prof. Fan Liu’s lab at FMP Berlin, focusing on learning cross-linking mass spectrometry to study protein-protein interactions and protein structures on a larger scale. I then spent two years as research staff in the FMP mass spectrometry core facility, managing instruments and technicians while providing experimental support for internal and external user projects.
Bogdanow, B., Ruwolt, M., Ruta, J., Mühlberg, L., Wang, C., Zeng, W.-F., Elofsson, A., Liu, F. (2024) Redesigning error control in cross-linking mass spectrometry enables more robust and sensitive protein-protein interaction studies. Molecular Systems Biology.
Clasen, M. A.*, Ruwolt, M.*, Wang, C., Ruta, J., Bogdanow, B., Kurt, L. U., Zhang, Z., Wang, S., Gozzo, F. C., Chen, T., Carvalho, P. C., Borges Lima, D., Liu, F. (2024) Proteome-scale recombinant standards and a robust high-speed search engine to advance cross-linking MS-based interactomics. Nature Methods. *these authors contributed equally
Kravčenko, U., Ruwolt, M., Kroll, J., Yushkevich, A., Zenkner, M., Ruta, J., Lotfy, R., Wanker, E. E., Rosenmund, C., Liu, F., Kudryashev, M. (2024) Molecular architecture of synaptic vesicles. PNAS.
Zhu, Y., Akkaya, K. C., Ruta, J., Yokoyama, N., Wang, C., Ruwolt, M., Borges Lima, D., Lehmann, M., Liu, F. (2024) Cross-link assisted spatial proteomics to map sub-organelle proteomes and membrane protein topologies. Nature Communications.
Ruwolt, M., Piazza, I., Liu, F. (2023) The potential of cross-linking mass spectrometry in the development of protein–protein interaction modulators (mini-review). Current Opinion in Structural Biology.
Ruwolt, M., He, Y., Borges Lima, D., Barshop, W., Broichhagen, J., Huguet, R., Viner, R., Liu, F. (2023) Real-Time Library Search Increases Cross-Link Identification Depth across All Levels of Sample Complexity. Analytical Chemistry.
Ruwolt, M., Schnirch, L., Borges Lima, D., Nadler-Holly, M., Viner, R., Liu, F. (2022) Optimized TMT-Based Quantitative Cross-Linking Mass Spectrometry Strategy for Large-Scale Interactomic Studies. Analytical Chemistry.
Keywords
- Cross-linking mass spectrometry, protein-protein interactions, protein-ligand interactions, proximity labelling, quantitative proteomics data analysis