1. Micrograph-based helix tracing (MicHelixTrace) using Spring

    Huber, S. T., Kuhm, T., Sachse, C. (2017). Automated tracing of helical assemblies from electron cryo-micrographs. J Struct Biol, in press.

  1. Review on single-particle based helical reconstruction

    Fromm, S. A., Sachse, C. (2016). Cryo-EM Structure Determination Using Segmented Helical Image Reconstruction. Meth Enzymol, 579: 307–328.

  1. Review on single-particle based helical reconstruction

    Sachse, C. (2015). Single-particle based helical reconstruction—how to make the most of real and Fourier space. AIMS Biophysics, 2(2), 219–244.

  1. Spring with direct electron detector data

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

  1. Spring (original publication)

    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.

  1. Prototype study using SPIDER

    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.

Examples of Spring structures

  • Denis Ptchelkine, Ashley Gillum, Tomohiro Mochizuki, Soizick Lucas-Staat, Ying Liu, Mart Krupovic, Simon E. V. Phillips, David Prangishvili & Juha T. Huiskonen (2017). Unique architecture of thermophilic archaeal virus APBV1 and its genome packaging. Nature Communications 8: 1436 (2017)
  • Manoël Prouteau, Ambroise Desfosses, Christian Sieben, Clélia Bourgoint, Nour Lydia Mozaffari, Davide Demurtas, Alok K. Mitra, Paul Guichard, Suliana Manley & Robbie Loewith (2017). TORC1 organized in inhibited domains (TOROIDs) regulate TORC1 activity. Nature 550, 265–269 (2017)
  • Hideyuki Matsunami, Clive S. Barker, Young-Ho Yoon, Matthias Wolf & Fadel Samatey (2016). Complete structure of the bacterial flagellar hook reveals extensive set of stabilizing interactions. Nature Communications 7: 13425 (2016)
  • Xabier Agirrezabala, Eduardo Méndez-López, Gorka Lasso, M Amelia Sánchez-Pina, Miguel Aranda, Mikel Valle (2015). The near-atomic cryoEM structure of a flexible filamentous plant virus shows homology of its coat protein with nucleoproteins of animal viruses. eLife 2015;4:e11795
  • Bharat T., Murshudov G., Sachse C., Löwe J. (2015). Structures of actin-like ParM filaments show architecture of plasmid-segregating spindles. Nature, 523(7558), 106–110..
  • 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.
  • 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.
  • 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 (New York, NY), 348(6235), 704–707.
  • 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.
  • 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.
  • Sachse, C., Fändrich, M., and Grigorieff, N. (2008). Paired beta-sheet structure of an Abeta(1-40) amyloid fibril revealed by electron microscopy. Proc Natl Acad Sci USA 105, 7462–7466.