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Previous and current research
Integrated structure determination approaches
Research in our laboratory combines biochemical approaches, proteomics and cryo-electron microscopy to study the structure and function of large macromolecular assemblies. Cryo-electron tomography is the ideal tool to observe molecular machines at work in their native environment (figure 1). Since the attainable resolution of the tomograms is moderate, the challenge ahead is to integrate information provided by complementary approaches in order to bridge the resolution gap towards high-resolution techniques (NMR, X-ray crystallography). Mass spectrometry approaches can provide the auxiliary information that is necessary to tackle this challenge. Targeted mass spectrometry can handle complex protein mixtures and, in combination with heavy labelled reference peptides, provides quantitative information about protein stoichiometries. Using this together with cross-linking techniques can reveal protein interfaces. The spatial information obtained in this way facilitates the fitting of high-resolution structures into cryo-EM maps in order to build pseudo-atomic models of entire molecular machines (figure 2).
Large macromolecular assemblies
Megadalton protein complexes are involved in a number of fundamental cellular processes such as cell division, vesicular trafficking and nucleocytoplasmic exchange. In most cases such molecular machines consist of a multitude of different proteins that occur in several copies within an individual assembly. Their function is often fine-tuned towards context specific needs by compositional remodelling across different cell-types. Structural variations occur through stoichiometric changes, subunit switches or competing protein interfaces. Studying the structure and function of Megadalton protein complexes is a challenging task, not only due to their compositional complexity but also because of their sheer size, which makes them inaccessible to biochemical purification.
Future projects and goals
To develop integrated workflows for structure determination of large macromolecular assemblies such as the nuclear pore complex (figure 2).
To reveal the function of cell-type specific variations of macromolecular assemblies.
Integrated structure determination approaches
Research in our laboratory combines biochemical approaches, proteomics and cryo-electron microscopy to study the structure and function of large macromolecular assemblies. Cryo-electron tomography is the ideal tool to observe molecular machines at work in their native environment (figure 1). Since the attainable resolution of the tomograms is moderate, the challenge ahead is to integrate information provided by complementary approaches in order to bridge the resolution gap towards high-resolution techniques (NMR, X-ray crystallography). Mass spectrometry approaches can provide the auxiliary information that is necessary to tackle this challenge. Targeted mass spectrometry can handle complex protein mixtures and, in combination with heavy labelled reference peptides, provides quantitative information about protein stoichiometries. Using this together with cross-linking techniques can reveal protein interfaces. The spatial information obtained in this way facilitates the fitting of high-resolution structures into cryo-EM maps in order to build pseudo-atomic models of entire molecular machines (figure 2).
Large macromolecular assemblies
Megadalton protein complexes are involved in a number of fundamental cellular processes such as cell division, vesicular trafficking and nucleocytoplasmic exchange. In most cases such molecular machines consist of a multitude of different proteins that occur in several copies within an individual assembly. Their function is often fine-tuned towards context specific needs by compositional remodelling across different cell-types. Structural variations occur through stoichiometric changes, subunit switches or competing protein interfaces. Studying the structure and function of Megadalton protein complexes is a challenging task, not only due to their compositional complexity but also because of their sheer size, which makes them inaccessible to biochemical purification.
Future projects and goals
To develop integrated workflows for structure determination of large macromolecular assemblies such as the nuclear pore complex (figure 2).
To reveal the function of cell-type specific variations of macromolecular assemblies.
研究兴趣
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Reiya Taniguchi,Clarisse Orniacki, Jan Philipp Kreysing,Vojtech Zila, Christian E. Zimmerli, Stefanie Boehm, Beata Turonova, Hans-Georg Kraeusslich,Valerie Doye,Martin Beck
biorxiv(2024)
Sergio Cruz-León, Tomáš Majtner, Patrick C Hoffmann, Jan Philipp Kreysing, Sebastian Kehl, Maarten W Tuijtel, Stefan L Schaefer, Katharina Geißler,Martin Beck, Beata Turoňová,Gerhard Hummer
Nature communicationsno. 1 (2024): 3992-3992
Maarten W Tuijtel, Sergio Cruz-León, Jan Philipp Kreysing,Sonja Welsch,Gerhard Hummer,Martin Beck,Beata Turoňová
Jan Philipp Kreysing,Maziar Heidari,Vojtech Zila, Sergio Cruz-Leon,Agnieszka Obarska-Kosinska,Vibor Laketa,Sonja Welsch,Juergen Koefinger,Beata Turonova,Gerhard Hummer, Hans-Georg Kraeusslich,Martin Beck
crossref(2024)
Patrick C Hoffmann, Hyuntae Kim, Agnieszka Obarska-Kosinska, Jan Philipp Kreysing, Eli Andino-Frydman, Sergio Cruz-Leon, Lenka Cernikova,Jan Kosinski,Beata Turonova, Gerhard Hummer,Martin Beck
biorxiv(2024)
Marie Stampe Ostenfeld,Dennis K. Jeppesen, Jens R. Laurberg,Anders T. Boysen,Jesper B. Bramsen, Bjarke Primdal-Bengtson,An Hendrix,Philippe Lamy,Frederik Dagnaes-Hansen,Mads H. Rasmussen, Khan H. Bui,Niels Fristrup,
crossref(2023)
Acta Crystallographicano. a1 (2023): A323-A323
crossref(2023)
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