November 19, 2019


All publications from the Sachse lab on Pubmed. For more details on publication statistics and metrics, follow us on Google Scholar, Web of Science and


    • 71. Berkamp, S., Daviran, D., Smeets, M., Caignard, A., jani, R., Sundermeyer, P., Jonker, C., Gerlach, S., Hoffmann, B., Lau, K. and Sachse, C. (2023). Correlative Light and Electron Cryo-Microscopy Workflow Combining Micropatterning, Ice Shield, and an In-Chamber Fluorescence Light Microscope. Bio-protocol 13(24): e4901
    • 70. Furthmann, N., Bader, V., Angersbach, L., Blusch, A., Goel, S., Sánchez-Vicente, A., Krause, L.J., Chaban, S.A., … Sachse, C., …, et al. (2023). NEMO reshapes the α-Synuclein aggregate interface and acts as an autophagy adapter by co-condensation with p62. Nat Commun 14, 8368. 
    • 69. Mann, D., Fromm, S.A., Martinez-Sanchez, A., Gopaldass, N., Choy, R., Mayer, A., and Sachse, C. (2023). Atg18 oligomer organization in assembled tubes and on lipid membrane scaffolds. Nat Commun 14, 8086
    • 68. Schlösser, L., Sachse, C., Low, H.H., and Schneider, D. (2023). Conserved structures of ESCRT-III superfamily members across domains of life. Trends in Biochemical Sciences, S0968000423002128. 10.1016/j.tibs.2023.08.009.
    • 67. Leidl, M. L., Sachse, C., and Müller-Caspary, K. (2023) Dynamical scattering in ice-embedded proteins in conventional and scanning transmission electron microscopy. IUCrJ. 10, 475–486
    • 66. Sachse, K., Hölzer, M., Vorimore, F., Barf, L.-M., Sachse, C., Laroucau, K., Marz, M., and Lamkiewicz, K. (2023) Genomic analysis of 61 Chlamydia psittaci strains reveals extensive divergence associated with host preference. BMC Genomics. 24, 288
    • 65. Ortmann De Percin Northumberland, C., and Sachse, C. (2023) Eiskalte Schnappschüsse von Biomolekülen: Kryo‐Elektronenmikroskopie. Physik in unserer Zeit. 54, 116–123
    • 64. Gewehr, L., Junglas, B., Jilly, R., Franz, J., Zhu, W. E., Weidner, T., Bonn, M., Sachse, C., and Schneider, D. (2023) SynDLP is a dynamin-like protein of Synechocystis sp. PCC 6803 with eukaryotic features. Nat Commun. 14, 2156


    • 63. Lazić, I., and Sachse, C. Obtaining cryo-EM structures by scanning transmission electron microscopy. (2022) Nat Briefing
    • 62. Lazić I., Wirix M., Leidl M.L., de Haas F, Mann D., Beckers M., Pechnikova E.V., Müller-Caspary K., Egoavil R., Bosch E.G.T., Sachse C. Single-particle cryo-EM structures from iDPC-STEM at near-atomic resolution. (2022) Nat Methods 19(9):1126-1136


    • 61. Junglas B., Huber S.T., Heidler T., Schlösser R., Mann D., Hennig R., Clarke M., Hellmann N., Schneider D. and Sachse C. PspA adopts an ESCRT-III-like fold and remodels bacterial membranes. (2021) Cell 184(14): 3674–3688.e18.
    • 60. Siebenaller, C., Schlösser, L., Junglas, B., Schmidt-Dengler, M., Jacob, D., Hellmann, N., Sachse, C., Helm, M., and Schneider, D. Binding and/or hydrolysis of purine-based nucleotides is not required for IM30 ring formation. (2021) FEBS Lett.
    • 59. Dunin-Borkowski R.E., Mayer J., Sachse C., and Tillmann K. Introduction to a special issue on Frontiers of Aberration Corrected Electron Microscopy in honour of Wolfgang Baumeister, Colin Humphreys, John Spence and Knut Urban on the occasion of their 75th, 80th, 75th and 80th birthdays. (2021) Ultramicroscopy 229:1.
    • 58. Klionsky, D. J., … Sachse, C. … et al. Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition). (2021) Autophagy, 17(1), 1–382.
    • 57. Beckers M., Mann D., and Sachse C. Structural interpretation of cryo-EM image reconstructions. (2021) Prog Biophys Mol Biol. doi:10.1016/j.pbiomolbio.2020.07.004.


    • 55. Huber S.T., Mostafavi S., Mortensen S.A., Sachse C. Structure and assembly of ESCRT-III helical Vps24 filaments. (2020) Sci Advances 6(34): eaba4897.

    • 54. Beckers M., and Sachse C. Permutation testing of Fourier shell correlation for resolution estimation of cryo-EM maps. (2020) J Struct Biol:107579.

    • 52. Jakobi A.J., Huber S.T., Mortensen S.A., Schultz S.W., Palara A., Kuhm T., Shrestha B.K., Lamark T., Hagen W.J.H., Wilmanns M., Johansen T., Brech A., and Sachse C. (2020) Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake. Nat Commun 11(1):440.


    • 51. Weis F., Beckers M., von der Hocht I., Sachse C. (2019) Elucidation of viral disassembly switch of tobacco mosaic virus. EMBO Reports 20(11):e48451.

    • 50. Krueger D., Quinkler T., Mortensen S.A., Sachse C., De Renzis, S. (2019) Crosslinker regulation of actin network topology controls tissue morphogenesis. J Biol Chem 218(8):2743-2761.

    • 49. Dunin-Borkowski R.E., Mayer J., Sachse C., and Tillmann K. (2019) Introduction to a special issue on Frontiers of Aberration Corrected Electron Microscopy in honour of Christian Colliex, Archie Howie and Hannes Lichte on the occasion of their 75th, 85th and 75th birthdays. Ultramicroscopy 203:1.

    • 48. Horos R., Büscher M., Sachse C., and Hentze M.W. Vault RNA emerges as a regulator of selective autophagy. (2019) Autophagy 15(8):1463-1464.

    • 47. Horos R., Büscher M., Kleinendorst R., Alleaume A.-M., Tarafder A.K., Schwarzl T., Dziuba D., Tischer C., Zielonka E.M., Adak A., Castello A., Huber W., Sachse C., and Hentze M.W. (2019) The Small Non-coding Vault RNA1-1 Acts as a Riboregulator of Autophagy. Cell 176(5):1054–1067.e12.

    • 46. Tarafder, A.K., Guesdon, A., Kuhm, T., Sachse, C. (2019) Recombinant Expression, Purification and Assembly of p62 Filaments. Methods Mol Biol. 1880:3-15.

    • 45. Beckers, M., Jakobi, A. J., Sachse, C. (2019) Thresholding of cryo-EM density maps by false discovery rate control. IUCr Journal 6 (1).


    • 43. Pellegrini, E. Desfosses, A., Wallmann, A., Schulze, W. M., Rehbein, K., Mas, L. Signor, P., Gaudon, S., Zenkeviciute, G., Hons, M., Malet, H., Gutsche, I., Sachse, C., Schoehn, G., Oschkinat, H., and Cusack, S. RIP2 filament formation is required for NOD2 dependent NF-κB signalling. (2018) Nat Commun, 9, (1) 4043.

    • 42. Zaffagnini, G., Savova., A., Danieli, A., Romanov, J., Tremel, S., Ebner, M., Peterbauer, T., Sztacho, M., Trapannone, R., Tarafder, A. K., Sachse, C. and Martens, S. Phasing out the bad-How SQSTM1/p62 sequesters ubiquitinated proteins for degradation by autophagy. (2018) Autophagy, 14 (7) 1280–1282.

    • 41. Zaffagnini, G., Savova., A., Danieli, A., Romanov, J., Tremel, S., Ebner, M., Peterbauer, T., Sztacho, M., Trapannone, R., Tarafder, A. K., Sachse, C. and Martens, S. p62 filaments capture and present ubiquitinated cargos for autophagy. (2018) EMBO J, p. e98308.

    • 40. Huber, S. T., Kuhm, T., Sachse, C. Automated tracing of helical assemblies from electron cryo-micrographs. (2018) J Struct Biol, 202 (1) 1–12.


    • 39. Jakobi, A. J., Wilmanns, M., and Sachse, C. (2017). Model-based local density sharpening of cryo-EM maps. eLife; 6:e27131.

    • 38. Sadian, Y., Tafur, L., Kosinski, J., Jakobi, A. J., Wetzel, R., Buczak, K., Hagen, W. J., Beck, M., Sachse, C., and Müller, C. W., Structural insights into transcription initiation by yeast RNA polymerase I. EMBO J, 36, (18) 2698–2709.

    • 37. Kolovou, A. , Schorb, M., Tarafder, A., Sachse, C., Schwab, Y., Santarella-Mellwig, R. (2017) A new method for cryo-sectioning cell monolayers using a correlative workflow. Methods Cell Biol., 140, 85–103.

    • 36. Dauden, M. I., Kosinski, J., Kolaj-Robin, O., Desfosses, A., Ori, A., Faux, C., Hoffmann, N. A., Onuma, O. F., Breunig, K. D., Beck, M., Sachse, C., Seraphin, B., Glatt, S. & Müller, C. W. (2017). Architecture of the yeast Elongator complex. EMBO Rep,18(2) 264–279.


    • 35. Tafur, L., Sadian, Y., Hoffmann, N. A., Jakobi, A. J., Wetzel, R., Hagen, W. J. H., Sachse, C., & Müller, C. W. (2016). Molecular Structures of Transcribing RNA Polymerase I. Mol Cell, 64(6) 1135–1143.

    • 34. Ohashi Y., Soler N., Garcia Ortegon M., Zhang L., Kirsten M. L., Perisic O., Masson G. R., Burke J. E., Jakobi A.J., Apostolakis A. A., Johnson C. M., Ohashi M., Ktistakis N. T., Sachse C., Williams R. L. (2016). Characterization of Atg38 and NRBF2, a fifth subunit of the autophagic Vps34 complex. Autophagy, 12(11), 2129–2144.

    • 33. Schur, F.K.M., Obr, M., Hagen, W.J.H., Wan, W., Jakobi, A.J., Kirkpatrick, J.M., Sachse, C., Kräusslich, H.-G., Briggs J.A.G. (2016). An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation. (2016). An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation. Science, 353(6298), 506–508.

    • 31. Bertipaglia, C., Schneider, S., Tarafder, A. K., Jakobi, A. J., Bykov, Y. S., Picco, A., Kukulski W., Konsinski J., Hagen W.J.H., Wilmanns M., Briggs, J.A.G., Sachse, C. (2016). Higher-order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the Cvt vesicle. EMBO Rep, 17(7), 1044–1060.

    • 30. Hoffmann, N. A., Jakobi, A. J., Vorländer, M. K., Sachse, C., & Müller, C. W. (2016). Transcribing RNA polymerase III observed by electron cryo-microscopy. FEBS J, 283(15), 2811–2819.

    • 29. Klionsky, D. J., Abdelmohsen, K., Abe, A., Abedin, M. J., … Sachse, C. … et al. (2016). Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy, 12(1), 1–222.


    • 28. Hoffmann, N. A., Jakobi, A. J., Moreno-Morcillo, M., Glatt, S., Kosinski, J., Hagen, W. J. H., Sachse, C., Müller C. W. (2015). Molecular structures of unbound and transcribing RNA polymerase III. Nature, 528(7581), 231–236.

    • 25. Bharat, T.A.M., Murshudov, G.N., Sachse, C., and Löwe, J. (2015). Structures of actin-like ParM filaments show architecture of plasmid-segregating spindles. Nature, 523(7558), 106–110.

    • 24. Ciuffa R., Lamark T., Tarafder A., Guesdon A., Rybina S., Hagen W.J.H., Johansen T., Sachse C. (2015). The selective autophagy receptor p62 forms a flexible filamentous helical scaffold. Cell reports, 11(5), 748–758.

    • 23. Skruzny M., Desfosses A., Prinz S., Dodonova S.O., Gieras A., Uetrecht C., Jakobi A.J., Abella M., Hagen W.J.H., Schulz J., Meijers R., Rybin V., Briggs J.A.G., Sachse C., Kaksonen M., (2015). An organized co-assembly of clathrin adaptors is essential for endocytosis. Developmental cell, 33(2), 150–162.

    • 22. Gutsche, I., Desfosses, A., Effantin, G., Ling, W.L., Haupt, M., Ruigrok, R.W.H., Sachse, C., and Schoehn, G. (2015). Near-atomic cryo-EM structure of the helical measles virus nucleocapsid. Science, 348(6235), 704–707.

    • 21. Ehebauer, M.T., Zimmermann, M., Jakobi, A.J., Noens, E.E., Laubitz, D., Cichocki, B., Marrakchi, H., Lanéelle, M.-A., Daffé, M., Sachse, C., et al. (2015). Characterization of the Mycobacterial Acyl-CoA Carboxylase Holo Complexes Reveals Their Functional Expansion into Amino Acid Catabolism. PLoS Pathog 11, e1004623.

    • 20. Fromm, S.A., Bharat, T.A.M., Jakobi, A.J., Hagen, W.J.H., and Sachse, C. (2015). Seeing tobacco mosaic virus through direct electron detectors. J Struct Biol 189, 87–97.

    • 19. Elad, N., De Strooper, B., Lismont, S., Hagen, W., Veugelen, S., Arimon, M., Horre, K., Berezovska, O., Sachse, C., and Chavez-Gutierrez, L. (2015). The dynamic conformational landscape of  γ-secretase. J Cell Sci 128, 589–598.


    • 18. Vahokoski, J., Bhargav, S.P., Desfosses, A., Andreadaki, M., Kumpula, E.-P., Martinez, S.M., Ignatev, A., Lepper, S., Frischknecht, F., Sidén-Kiamos, I., Sachse, C. and Kursula, I. (2014). Structural differences explain diverse functions of Plasmodium actins. PLoS Pathog 10, e1004091.

    • 17. Afonin, S., Glaser, R.W., Sachse, C., Salgado, J., Wadhwani, P., and Ulrich, A.S. (2014). (19)F NMR screening of unrelated antimicrobial peptides shows that membrane interactions are largely governed by lipids. Biochim Biophys Acta 1838, 2260–2268.

    • 16. Desfosses, A., Ciuffa, R., Gutsche, I., and Sachse, C. (2014). SPRING – an image processing package for single-particle based helical reconstruction from electron cryomicrographs. J Struct Biol 185, 15–26.


    • 15. Gombos, L., Neuner, A., Berynskyy, M., Fava, L.L., Wade, R.C., Sachse, C., and Schiebel, E. (2013). GTP regulates the microtubule nucleation activity of γ-tubulin. Nat Cell Biol 15, 1317–1327.


    • 14. Bharat, T.A.M., Davey, N.E., Ulbrich, P., Riches, J.D., de Marco, A., Rumlova, M., Sachse, C., Ruml, T., and Briggs, J.A.G. (2012). Structure of the immature retroviral capsid at 8 Å resolution by cryo-electron microscopy. Nature 487, 385–389.

    • 13. Guichard, P., Desfosses, A., Maheshwari, A., Hachet, V., Dietrich, C., Brune, A., Ishikawa, T., Sachse, C., and Gönczy, P. (2012). Cartwheel architecture of Trichonympha basal body. Science 337, 553.


    • 12. Korkhov, V.M., Sachse, C., Short, J.M., and Tate, C.G. (2010). Three-dimensional structure of TspO by electron cryomicroscopy of helical crystals. Structure 18, 677–687.

    • 11. Sachse, C., Grigorieff, N., and Fändrich, M. (2010). Nanoscale flexibility parameters of Alzheimer amyloid fibrils determined by electron cryo-microscopy. Angew Chem Int Ed Engl 49, 1321–1323.


    • 10. Low, H.H., Sachse, C., Amos, L.A., and Löwe, J. (2009). Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving. Cell 139, 1342–1352.

    • 9. Meinhardt, J., Sachse, C., Hortschansky, P., Grigorieff, N., and Fändrich, M. (2009). Abeta(1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. J Mol Biol 386, 869–877.

    • 8. Schmidt, M., Sachse, C., Richter, W., Xu, C., Fändrich, M., and Grigorieff, N. (2009). Comparison of Alzheimer Abeta(1-40) and Abeta(1-42) amyloid fibrils reveals similar protofilament structures. Proc Natl Acad Sci USA 106, 19813–19818.


    • 7. Chen, J.Z., Sachse, C., Xu, C., Mielke, T., Spahn, C.M.T., and Grigorieff, N. (2008). A dose-rate effect in single-particle electron microscopy. J Struct Biol 161, 92–100.


    • 5. Habicht, G., Haupt, C., Friedrich, R.P., Hortschansky, P., Sachse, C., Meinhardt, J., Wieligmann, K., Gellermann, G.P., Brodhun, M., Götz, J., et al. (2007). Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils. Proc Natl Acad Sci USA 104, 19232–19237.

    • 4. Sachse, C., Chen, J.Z., Coureux, P.-D., Stroupe, M.E., Fändrich, M., and Grigorieff, N. (2007). High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus. J Mol Biol 371, 812–835.


    • 3. Sachse, C., Xu, C., Wieligmann, K., Diekmann, S., Grigorieff, N., and Fändrich, M. (2006). Quaternary structure of a mature amyloid fibril from Alzheimer’s Abeta(1-40) peptide. J Mol Biol 362, 347–354.


    • 2. Glaser, R.W., Sachse, C., Dürr, U.H.N., Wadhwani, P., Afonin, S., Strandberg, E., and Ulrich, A.S. (2005). Concentration-dependent realignment of the antimicrobial peptide PGLa in lipid membranes observed by solid-state 19F-NMR. Biophys. J. 88, 3392–3397.


    • 1. Glaser, R.W., Sachse, C., Dürr, U.H.N., Wadhwani, P., and Ulrich, A.S. (2004). Orientation of the antimicrobial peptide PGLa in lipid membranes determined from 19F-NMR dipolar couplings of 4-CF3-phenylglycine labels. J. Magn. Reson. 168, 153–163.