Christian Tüting
Martin Luther University of Halle-Wittenberg
25 Papers
30 Citations
Christian Tüting is an academic researcher from Martin Luther University of Halle-Wittenberg. The author has contributed to research in topics: Biology & Chemistry. The author has an hindex of 4, co-authored 10 publications.
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Papers
Integrative structure of a 10-megadalton eukaryotic pyruvate dehydrogenase complex from native cell extracts.
Fotis L. Kyrilis,Dmitry A. Semchonok,Ioannis Skalidis,Christian Tüting,Farzad Hamdi,Francis J. O’Reilly,Juri Rappsilber,Panagiotis L. Kastritis +7 more
TL;DR: The pyruvate dehydrogenase complex (PDHc) is a giant enzymatic assembly involved in pyruvanate oxidation as mentioned in this paper, and its quaternary structure has remained elusive due to sheer size, heterogeneity, and plasticity.
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Cryo-EM and artificial intelligence visualize endogenous protein community members.
Ioannis Skalidis,Fotis L. Kyrilis,Christian Tüting,Farzad Hamdi,Grzegorz Chojnowski,Panagiotis L. Kastritis +5 more
TL;DR: In this paper , the structure of a 60S pre-ribosome, fatty acid synthase, and pyruvate/oxoglutarate dehydrogenase complex E2 cores is characterized using 3.84-4.52 Å resolution by collecting <3,000 micrographs of a single cellular fraction.
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Reconstitution of 3′ end processing of mammalian pre-mRNA reveals a central role of RBBP6
Moritz Schmidt,F Kluge,Felix Sandmeir,Uwe Kühn,Peter Schäfer,Christian Tüting,Christian Ihling,Elena Conti,Elmar Wahle +8 more
TL;DR: Here, Schmidt et al. reconstituted the endonucleolytic cleavage of an extended precursor followed by the addition of a poly(A) tail reaction from overproduced and purified proteins, and provide a minimal list of 14 polypeptides that are essential and two that are stimulatory for RNA processing.
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Cryo-EM snapshots of a native lysate provide structural insights into a metabolon-embedded transacetylase reaction.
Christian Tüting,Fotis L. Kyrilis,Johannes Müller,Marija Sorokina,Ioannis Skalidis,Farzad Hamdi,Yashar Sadian,Panagiotis L. Kastritis +7 more
TL;DR: In this paper, the structure of the fully active Chaetomium thermophilum pyruvate dehydrogenase complex (PDHc) core scaffold at 3.85 µm resolution (FSC) was reported from native cell extracts.
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Structural analysis of 70S ribosomes by cross-linking/mass spectrometry reveals conformational plasticity.
TL;DR: This working model explains more than 95% of all cross-links, resulting in an optimized E. coli ribosome structure based on the cross-linking data obtained, and might serve as benchmark for conducting biochemical experiments on newly modeled protein regions, guided by XL-MS.