Service Project Z02

Single-particle cryo-EM infrastructure

Principle Investigator: Lukas Sušac, Tatjana Schusser, Martin Beck, Robert Tampé

Research Areas: Structural Biology, Single-particle cryo-EM


The major aim of the high-resolution imaging platform (Z) is to provide access to state-of-the- art cryogenic electron microcopy (cryo-EM) to the members of the Collaborative Research Center. By offering technical expertise and extensive methodological know-how, the Z project enables CRC projects to benefit from the unrivaled capabilities of cryo-EM to illuminate macromolecular structure and function. In addition, the service project will train the next generation of cryo-EM microscopists among the researchers and students of the CRC, and beyond. Finally, the Z project will also devote substantial efforts to the development of new approaches for sample preparation and screening. The central infrastructure will provide a decisive technological advantage to all projects of the CRC by delivering unique, high- resolution insights into the molecular membrane biology via cryo-EM imaging that will substantially contribute to the success of the CRC.

Download: User instructions


Dr. Lukas Sušac

Scientific Coordination of high-resolution cryo-EM infrastructure

Tatjana Schusser

Application Specialist Electron Microscopy


  1. Sekulovski S, Sušac L, Stelzl LS, Tampé R, Trowitzsch S (2023) Structural basis of substrate recognition by human tRNA splicing endonuclease TSEN. Nat Struct Mol Biol 30: 834-840
  2. Sušac L, Young MT, Thomas C, von Bülow S, O’Brien-Ball C, Santos AM, Fernandes RA, Hummer G, Tampé R*, Davis SJ* (2022) Structure of a fully assembled tumor-specific T-cell receptor ligated by pMHC. Cell 185: 3201-13
  3. He Y, Wang Y, Liu B, Helmling C, Sušac L, Cheng R, Zhou ZH, Feigon J (2021) Structure of telomerase at several steps of telomere repeat synthesis. Nature 593: 453-9
  4. Allegretti M, Zimmerli CE, Rantos V, Wilfling F, Ronchi P, Fung HKH, Lee CW, Hagen W, Turoňová B, Karius K, Börmel M, Zhang X, Müller C, Schwab Y, Mahamid J, Pfander B, Kosinski J, Beck M (2020) In-cell architecture of the nuclear pore complex and snapshots of its turnover. Nature 586: 796–800
  5. Hofmann S, Januliene D, Mehdipour AR, Thomas C, Stefan E, Brüchert S, Kuhn BT, Geertsma ER, Hummer G, Tampé R*, Moeller A* (2019) Conformation space of a heterodimeric ABC exporter under turnover conditions. Nature 471: 580-3
  6. Hampoelz B, Schwarz A, Ronchi P, Bragulat-Teixidor H, Tischer C, Gaspar I, Ephrussi A, Schwab Y, Beck M (2019) Nuclear pores assemble from nucleoporin condensates during oogenesis. Cell 179: 671-86
  7. Jiang J*, Wang Y*, Sušac L*, Chan H, Basu R, Zhou ZH, Feigon J (2018) Structure of telomerase with telomeric DNA. Cell 173: 1179-90
  8. Sušac L, Eddy MT, Diderko T, Stevens RC, Wüthrich K (2018) A2A adenosine receptor functional states characterized by 19F-NMR. Proc Natl Acad Sci USA 115: 12722-28
  9. Blees A, Januliene D, Hofmann T, Koller N, Schmidt C, Trowitzsch S, Moeller A, Tampé R (2017) Structure of the human MHC-I peptide-loading complex. Nature 551: 525-8
  10. Heuer A, Gerovac M, Schmidt C, Trowitzsch S, Preis A, Kötter P, Berninghausen O, Becker T, Beckmann R, Tampé R (2017) Structure of the 40S-ABCE1 post-splitting complex in ribosome recycling and translation initiation. Nat Struct Mol Biol 24, 453-60
*corresponding author