Latest news:

Jul 10, 2021:
Our new JBC review on amyloid fibril structure determination by cryo-EM is out! HERE

Jul 10, 2021:
New preprint on bioRxiv: We present fibril structures of alpha-synuclein amplified from the brain of Parkinson and MSA patients: HERE

May 7, 2021:
Congratulations Christine on your excellent PhD defense!!

Sep 25, 2020:
New paper on biosensor engineering is out in Nat Commun, see HERE

Jun 15, 2020:
IAPP fibril paper is out in NSMB: HERE

Feb 12, 2020:
New preprint on bioRxiv: Amyloid fibril structure of islet amyloid polypeptide by cryo-electron microscopy reveals similarities with amyloid beta

Aug 21, 2019:
New publication in Nature Communications on the PI3K-SH3 amyloid fibril structure by Cryo-EM. see here.

Aug 7, 2019:
New DireX Version 0.7.1. Added a turbo mode, which is much faster (but less accurate). Download here.

Sep 10, 2017:
New publication in Science on the Abeta(1-42) fibril structure. see here.

Sep 1, 2017:
We have new job openings for postdocs and PhD students, see here.

Jul 10, 2017:
Congratulations to Michaela, Amudha, and Tatjana on their successful PhD Defenses!

Dec 4, 2015:
Congratulations to Dennis on his successfull PhD Defense!

Nov 22, 2015:
New publications on our protein structure refinement method and CASP11 results.

Feb 3, 2015:
Congratulations to Zhe on his successfull PhD Defense!



70. Benedikt Frieg, Leif Antonschmidt, Christian Dienemann, James A. Geraets, Eszter E. Najbauer, Dirk Matthes, Bert L. de Groot, Loren B. Andreas, Stefan Becker, Christian Griesinger, and Gunnar F. Schröder. The 3D structure of lipidic fibrils of α-synuclein.
Nat Commun , accepted
69. Benedikt Frieg, James A. Geraets, Timo Strohäker, Christian Dienemann, Panagiota Mavroeidi, Byung Chul Jung, Woojin S. Kim, Seung-Jae Lee, Maria Xilouri, Markus Zweckstetter, and Gunnar F. Schröder. Quaternary structure of patient-homogenate amplified α-synuclein fibrils modulates seeding of endogenous α-synuclein.
Commun Biol , accepted
68. L. Antonschmidt, D. Matthes, R. Dervişoğlu, B. Frieg, C. Dienemann, A. Leonov, E. Nimerovsky, V. Sant, S. Ryazanov, A. Giese, G. F. Schröder, S. Becker, B. L. de Groot, C. Griesinger, L. B. Andreas. The clinical drug candidate anle138b binds in a cavity of lipidic α-synuclein fibrils.
Nat Commun , accepted
67. Alain Ibáñez de Opakua, James A. Geraets, Benedikt Frieg, Christian Dienemann, Adriana Savastano, Marija Rankovic, Maria-Sol Cima-Omori, Gunnar F. Schröder, and M. Zweckstetter. Molecular interactions of FG nucleoporin repeats at high resolution.
Nat Chem , accepted
66. Zinke M, Schröder GF, Lange A. Major tail proteins of bacteriophages of the order Caudovirales.
J Biol Chem (2022) 298(1):101472


65. Conformational heterogeneity coupled with β-fibril formation of a scaffold protein involved in chronic mental illnesses. Cukkemane A, Becker N, Zielinski M, Frieg B, Lakomek NA, Heise H, Schröder GF, Willbold D, Weiergräber OH.
Transl Psychiatry(2021) 11(1):639
64. M.P. Schützmann, F. Hasecke, S. Bachmann, M. Zielinski, S. Hänsch, G.F. Schröder, H. Zempel, W. Hoyer.
Endo-lysosomal Aβ concentration and pH enable formation of Aβ oligomers that potently induce Tau missorting.
Nat Commun (2021) 12, 4634
or on bioRxiv:
63. M. Zielinski, C. Röder, G.F. Schröder. Challenges in sample preparation and structure determination of amyloids by cryo-EM.
JBC Reviews (2021) 297, ISSUE 2, 100938
62. D. Willbold, B. Strodel, G.F. Schröder, W. Hoyer, and H. Heise. Amyloid-type Protein Aggregation and Prion-like Properties of Amyloids.
Chem. Rev. (2021) 121, 13, 8285–8307
61. M Pagnon de la Vega, V. Giedraitis, W. Michno, L. Kilander, G. Güner, M. Zielinski, M. Löwenmark, R. Brundin, T. Danfors, L. Söderberg, I. Alafuzoff, L.N.G. Nilsson, A. Erlandsson, D. Willbold, S.A. Müller, G.F. Schröder, J. Hanrieder, S.F. Lichtenthaler, L. Lannfelt, D. Sehlin, M. Ingelsson. The Uppsala APP deletion causes early onset autosomal dominant Alzheimer’s disease by altering APP processing and increasing amyloid-β fibril formation.
Sci. Transl. Med. 13, eabc6184 (2021)
60. Pothula KR, Geraets JA, Ferber II, Schröder GF. Clustering polymorphs of tau and IAPP fibrils with the CHEP algorithm.
Prog Biophys Mol Biol. (2021) 160:16-25.
59. Lawson CL, Kryshtafovych A, Adams PD, Afonine PV, Baker ML, Barad BA, Bond P, Burnley T, Cao R, Cheng J, Chojnowski G, Cowtan K, Dill KA, DiMaio F, Farrell DP, Fraser JS, Herzik MA Jr, Hoh SW, Hou J, Hung LW, Igaev M, Joseph AP, Kihara D, Kumar D, Mittal S, Monastyrskyy B, Olek M, Palmer CM, Patwardhan A, Perez A, Pfab J, Pintilie GD, Richardson JS, Rosenthal PB, Sarkar D, Schäfer LU, Schmid MF, Schröder GF, Shekhar M, Si D, Singharoy A, Terashi G, Terwilliger TC, Vaiana A, Wang L, Wang Z, Wankowicz SA, Williams CJ, Winn M, Wu T, Yu X, Zhang K, Berman HM, Chiu W. Cryo-EM model validation recommendations based on outcomes of the 2019 EMDataResource challenge.
Nat Methods (2021) 18(2):156-164.


58. Cristina Risi, Luisa U. Schäfer, Betty Belknap, Ian Pepper, Howard D. White, Gunnar F. Schröder, and Vitold E. Galkin High-resolution cryo-EM structure of the cardiac actomyosin complex.
Structure (2020), accepted
57. Maximilian Zinke, Katrin A. A. Sachowsky, Carl Öster, Sophie Zinn-Justin, Raimond B.G. Ravelli, Gunnar F. Schröder, Michael Habeck, Adam Lange. Spinal Column Architecture of the Flexible SPP1 Bacteriophage Tail Tube
Nat Commun 11,5759 (2020)
See Press Release (english)
and Pressemitteilung (deutsch)
56. D. Della Corte, H. van Beek, F. Syberg, M. Schallmey, F. Tobola, K. Cormann, C. Schlicker, P. Baumann, K. Krumbach, S. Sokolowsky, C. Morris, A. Grünberger, E. Hofmann, G.F. Schröder, J. Marienhagen. Engineering and application of a biosensor with focused ligand specificity"
Nat Commun (2020) 11,4851.
See Press Release (english)
Pressemitteilung (deutsch)
55. O. Fisette, G.F. Schröder, L.V. Schäfer. Atomistic structure and dynamics of the human MHC-I peptide-loading complex
PNAS (2020), 117 (34) 20597-20606
See Press Release
54. C. Röder, T. Kupreichyk, L. Gremer, L.U. Schäfer, K.R. Pothula, R.B.G. Ravelli, D. Willbold, W. Hoyer and G.F. Schröder. Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with Aβ fibrils
Nat Struct Mol Biol (2020) 27:660–667
See Press Release (english)
und Pressemitteilung (deutsch)
53. James A. Geraets, Karunakar R. Pothula and Gunnar F. Schröder Integrating cryo-EM and NMR data
Curr Opin Struct Biol (2020) 61:173–181


52. C. Röder, N. Vettore, L. N. Mangels, L. Gremer, R.B.G. Ravelli, D. Willbold, W. Hoyer, A.K. Buell, G.F. Schröder Atomic structure of PI3-kinase SH3 amyloid fibrils by cryo-electron microscopy
Nat. Commun. 10, Article number: 3754 (2019)
Download data here:
Density Map (EMD-4727) and PDB Model (PDB ID 6R4R).
51. Marcel Falke, Julian Victor, Michael M. Wördehoff, Alessia Peduzzo, Tao Zhang, Gunnar F. Schröder, Alexander K. Buell, Wolfgang Hoyer, and Manuel Etzkorn. α-Synuclein-derived lipoparticles in the study of α-Synuclein amyloid fibril formation
Chem Phys Lipids (2019) 220:57–65


50. K. R. Pothula, D. Smyrnova, G. F. Schröder. Clustering cryo-EM images of helical protein polymers for helical reconstructions
Ultramicroscopy (2018) 203:132-138
49. C. Möckel, J. Kubiak, O. Schillinger, R. Kühnemuth, D. Della Corte, G. F. Schröder, D. Willbold, B. Strodel, C. A. M. Seidel, P. Neudecker. Integrated NMR, Fluorescence, and Molecular Dynamics Benchmark Study of Protein Mechanics and Hydrodynamics
J. Phys. Chem. B (2018) 123(7):1453-1480
48. C. Risi, B. Belknap, E. Forgacs-Lonart, S. P. Harris, G. F. Schröder, H. D. White, V. E. Galkin N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament
Structure (2018) 26:1-8


47. L. Gremer, D. Schölzel, C. Schenk, E. Reinartz, Jörg Labahn, R.B.G. Ravelli, M. Tusche, C. Lopez- Iglesias, W. Hoyer, H. Heise, D. Willbold, G.F. Schröder. Fibril structure of amyloid-ß(1-42) by cryo-electron microscopy
Science 358:116–119 (2017)
See Science Perspectives article by Popich and Raunser
46. A. Toulmin, L.E. Baltierra-Jasso, M.J. Morten, T. Sabir, P. McGlynn, G.F. Schröder, B.O. Smith, S.W. Magennis. Conformational heterogeneity in a fully-complementary DNA three-way junction with a GC-rich branchpoint
Biochemistry (2017) 56(37):4985-4991
45. C. Risi, J. Eisner, B. Belknap, D. H. Heeley, H. D. White, G. F. Schröder, V. E. Galkin. Ca2+-induced Movement of Tropomyosin on Native Cardiac Thin Filaments Revealed by Cryo Electron Microscopy
PNAS (2017) 114:6782-6787


44. N. Fischer, P. Neumann, L. V. Bock, C. Maracci, Z. Wang, A. Paleskava, A. L. Konevega, G. F. Schröder, H. Grubmüller, R. Ficner, M. V. Rodnina, and H. Stark. The pathway to GTPase activation of elongation factor SelB on the ribosome
Nature (2016) 540:80-85
43. E.A. Mirecka, S. Feuerstein, L. Gremer, G. F. Schröder, M. Stoldt, D. Willbold, and W. Hoyer. β-Hairpin of Islet Amyloid Polypeptide Bound to an Aggregation Inhibitor
Sci. Rep. (2016) 6, 33474
42. T. Braun, M. Vos, N. Kalisman, N. E. Sherman, R. Rachel, R. Wirth, G.F. Schröder, and E. Egelman. Archaeal Flagellin Combines a Bacterial Type IV Pilin Domain with an Immunoglobulin-like Domain
PNAS (2016) 113(37):10352-7


41. A. Wildberg, D. Della Corte, and G.F. Schröder. Coupling an ensemble of homologs improves refinement of protein homology models
J. Chem. Theo. Comput. (2015), 11(12):5578-5582
40. D. Della Corte, A. Wildberg, and G.F. Schröder. Protein Structure Refinement with Adaptively Restrained Homologous Replicas
Proteins (2015), doi:10.1002/prot.24939
39. M. Spiegel, A.K. Duraisamy, and G.F. Schröder. Improving the Visualisation of Cryo-EM Density Reconstructions
J.Struct.Biol. (2015), 191(2):207-213
38. T. Braun, A. Orlova, K. Valegård, A.-C. Lindås, G.F. Schröder, and E. H. Egelman. An Archaeal Actin from a Hyperthermophile Forms a Single-Stranded Filament
PNAS (2015), 112(30): 9340-9345.
37. A. Sali, H. M. Berman, T. Schwede, J. Trewhella, G. Kleywegt, S. K. Burley, J. Markley, H. Nakamura, P. Adams, A.M.J.J. Bonvin, W. Chiu, M. Dal Peraro, F. DiMaio, T. E. Ferrin, Kay Grünewald, A. Gutmanas, R. Henderson, G. Hummer, K. Iwasaki, G. Johnson, C. L. Lawson, J. Meiler, M. A. Marti-Renom, G. T. Montelione, M. Nilges, R. Nussinov, A. Patwardhan, J. Rappsilber, R. J. Read, H. Saibil, G.F. Schröder, C. Schwieters, C. A. M. Seidel, D. Svergun, M. Topf, E. L. Ulrich, S. Velankar, and J. D. Westbrook. Outcome of the First wwPDB Hybrid / Integrative Methods Task Force Workshop
Structure (2015) 23(7): 1156-1167.
36. G.F. Schröder. Hybrid Methods for Macromolecular Structure Determination: Experiment with Expectations
Curr. Opin. Struct. Biol. (2015) 31: 20-27. Click here to download
35. V.E. Galkin, A. Orlova, M.R. Vos, G.F. Schröder, and E.H. Egelman. Near-Atomic Resolution for One State of F-Actin
Structure (2015) 23(1): 173-182


34. G.F. Schröder, M.L. Levitt, and A.T. Brunger Deformable elastic network refinement for low-resolution macromolecular crystallography
Acta Cryst. D (2014) D70: 2241–2255
33. A. Lu, V.G. Magupalli, J. Ruan, Q. Yin, M.K. Atianand, M. Vos, G.F. Schröder, K.A. Fitzgerald, H. Wu, and E.H. Egelman Unified Polymerization Mechanism for the Assembly of ASC-Dependent Inflammasomes
Cell (2014) 156(6): 1193–1206
32. J. Kowal, M. Chami, P. Baumgartner, M. Arheit, P.-L. Chiu, M. Rangl, S. Scheuring, G.F. Schröder, C.M. Nimigean, H. Stahlberg. Ligand-induced structural changes in the cyclic nucleotide-modulated potassium channel MloK1
Nature Communications (2014) 5, 3106.


31. L.V. Bock, C. Blau, G.F. Schröder, I.I. Davydov, N. Fischer, H. Stark, M.V. Rodnina, A.C. Vaiana, and H. Grubmüller. Energy barriers and driving forces in tRNA translocation through the ribosome
Nat Struct Mol Biol (2013) 20:1390–1396
30. B. Falkner and G.F. Schröder. Cross-validation in cryo-electron microscopy based structural modeling
PNAS (2013) 110(22):8930-8935. [PDF]
29. D.-H. Chen, D. Madan, J. Weaver, Z. Lin, G.F. Schröder, W. Chiu, H.S. Rye. Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein
Cell (2013) 153:1354–1365. [PDF]
28. N. Kalisman, G.F. Schröder, M. Levitt. The Crystal Structures of the Eukaryotic Chaperonin CCT Reveal its Functional Partitioning
Structure (2013) 21:540–549. [PDF]
27. X. Deng, J. Morris, C. Chaton, G.F. Schröder, W.S. Davidson and T.B. Thompson. Small-angle X-ray Scattering of Apolipoprotein A-IV Reveals the Importance of Its Termini for Structural Stability
J. Biol. Chem. (2013) 288(7):4854-4866. [PDF]


26. X. Yu, C. Goforth, C. Meyer, R. Rachel, R. Wirth, G.F. Schröder, and E.H. Egelman. Filaments from Ignicoccus hospitalis Show Diversity of Packing in Proteins Containing N-terminal Type IV Pilin Helices.
J. Mol. Biol. (2012) 422(2): 274-281. [PDF]
25. A.T. Brunger, P.D. Adams, P. Fromme, R. Fromme, M. Levitt, and G.F. Schröder. Improving the accuracy of macromolecular structure refinement at 7 Å resolution.
Structure (2012), 20(6):957-966. [PDF]
24. T. Sabir, A. Toulmin, L. Ma, A.C. Jones, P. McGlynn, G.F. Schröder, and S.W. Magennis. Branchpoint expansion in a fully-complementary three-way DNA junction.
J. Am. Chem. Soc. (2012), 134(14):6280–6285. [PDF] ( See Cover)
23. Z. Wang, G.F. Schröder. Real-space Refinement with DireX: From Global Fitting to Side-chain Improvements.
Biopolymers (2012), 97(9):687-697. [PDF]
22. R. Henderson, A. Sali, M.L. Baker, B. Carragher, B. Devkota, K.H. Downing, E.H. Egelman, Z. Feng, J. Frank, N. Grigorieff, W. Jiang, S.J. Ludtke, O. Medalia, P.A. Penczek, P.B. Rosenthal, M.G. Rossmann, M.F. Schmid, G.F. Schröder, A.C. Steven, D.L. Stokes, J.D. Westbrook, W. Wriggers, H. Yang, J. Young, H.M. Berman, W. Chiu, G.J. Kleywegt, C.L. Lawson. Outcome of the First Electron Microscopy Validation Task Force Meeting.
Structure (2012) 20:205-214. [PDF]
21. D.J. O'Donovan, I. Stokes-Rees, Y. Nam, S. Blacklow, G.F. Schröder, A.T. Brunger, Piotr Sliz. A grid-enabled web service for low-resolution crystal structure refinement.
Acta Cryst. (2012) D68:268-276. [PDF]
20. A.T. Brunger, D. Das, A.M. Deacon, J. Grant, T.C. Terwilliger, R.J. Read, P.D. Adams, M. Levitt and G.F. Schröder. Application of DEN-Refinement And Automated Model-Building To A Difficult Case Of Molecular Replacement Phasing: The Structure Of A Putative Succinyl-Diaminopimelate Desuccinylase From Corynebacterium Glutamicum.
Acta Cryst. (2012). D68, 391-403 [PDF]


19. V.E. Galkin, A. Orlova, D. Kudryashov, A. Solodukhin, E. Reisler, G.F. Schröder, and E.H. Egelman. Remodeling of Actin Filaments by ADF/Cofilin Proteins.
PNAS (2011) 108(51):20568-20572 . [PDF]
18. S. Gao, A. von der Malsburg, A. Dick, K. Faelber, G.F. Schröder, O. Haller, G. Kochs, O. Daumke. Three domain architecture of dynamin-like MxA GTPase.
Immunity (2011) 35:514-525. [PDF]
17. Y. Cong, G.F. Schröder, A.S. Meyer, J. Jakana, B. Ma, M.T. Dougherty, M.F. Schmid, S. Reissmann, M. Levitt, S.L. Ludtke, J. Frydman, and W. Chiu. Symmetry-Free Cryo-EM Structures of the Chaperonin TRiC Along its ATPase-Driven Conformational Cycle.
EMBO J (2011) 31:720-730. [PDF]
16. E. Jaenicke, K. Büchler, H. Decker, J. Markl, T. Barends, and G.F. Schröder. The Refined Structure of Functional Unit h of Keyhole Limpet Hemocyanin (KLH1-h) Reveals Disulfide Bridges.
IUBMB Life (2011) 63(3):183-187. [PDF]
15. L. Zerrad, A. Merli, G.F. Schröder, A. Varga, E. Gráczer, P. Pernot, A. Round, M. Vas, and M.W. Bowler. A Spring Loaded Release Mechanism Regulates Domain Movement and Catalysis in Phosphoglycerate Kinase.
JBC (2011) 286:14040-14048. [PDF]
14. T. Sabir, G.F. Schröder, A. Toulmin, P. McGlynn, and S.W. Magennis. Global Structure of Forked DNA in Solution Revealed by High-Resolution Single-Molecule Fluorescence Resonance Energy Transfer.
J. Am. Chem. Soc. (2011) 133(5):1188-1191. [PDF]


13. V.E. Galkin, A. Orlova, G.F. Schröder, E.H. Egelman. Structural Polymorphism in F-actin.
Nat Struct Mol Biol (2010) 17:1318-1323. [PDF]
12. G.F. Schröder, M. Levitt, A.T. Brunger. Super-resolution biomolecular crystallography with low-resolution data.
Nature (2010) 464:1218-1222. [PDF]
See also "Preview" by Randy J. Read "From Poor Resolution to Rich Insight" Structure (2010) 18:664-665.
11. J. Zhang, M.L. Baker, G.F. Schröder, N.R. Douglas, S. Reissmann, J. Jakana, M. Dougherty, C.J. Fu, M. Levitt, S.J. Ludtke, J. Frydman, and W. Chiu. Mechanism of folding chamber closure in a group II chaperonin.
Nature (2010) 463:379-383. [PDF]

2001 - 2009

10. A. K. Wozniak, G.F. Schröder, H. Grubmüller, C.A.M. Seidel, F. Oesterhelt. Single molecule FRET measures bends and kinks in DNA.
PNAS (2008) 105(47):18337-18342. [PDF]
9. O.F. Lange, N.-A. Lakomek, C. Fares, G.F. Schröder, S. Becker, J. Meiler, H. Grubmüller, C. Griesinger, B.L. de Groot. Atomistic residual dipolar coupling ensemble of ubiquitin reveals molecular recognition dynamics up to the microsecond timescale.
Science (2008) 320:1471-1475. [PDF]
8. G.F. Schröder, A.T. Brunger, and M. Levitt. Combining Efficient Conformational Sampling with a Deformable Elastic Network Model Facilitates Structure Refinement at Low Resolution.
Structure (2007) 15:1630-1641. [PDF]
7. G. F. Schröder, U. Alexiev, and H. Grubmüller. Simulation of fluorescence anisotropy experiments Probing protein flexibility.
Biophys. J. (2005) 89:3757-3770. [PDF]
6. A. Wozniak, S. Nottrott, E. Kühn-Hölsken, G. F. Schröder, H. Grubmüller, R. Lührmann, A. M. Seidel and F. Oesterhelt. Detecting protein-induced folding of the U4 snRNA kinkturn by single-molecule multiparameter FRET measurements.
RNA (2005) 11:1545-1554. [PDF]
5. G.F. Schröder; Simulation of Fluorescence Spectroscopy Experiments , PhD Thesis, Universität Göttingen, 2004. [PDF]
4. M. Margittai, J. Widengren, E. Schweinberger, G.F. Schröder, S. Felekyan, E. Haustein, M. König, D. Fasshauer, H. Grubmüller, R. Jahn, and C. A. M. Seidel. Single-molecule fluorescence resonance energy transfer reveals a dynamic equilibrium between closed and open conformations of Syntaxin 1.
PNAS (2003) 100(26):15516-15521. [PDF]
3. G.F. Schröder and H. Grubmüller. Maximum likelihood trajectories from single molecule fluorescence resonance energy transfer experiments.
J. Chem. Phys. (2003) 119(18):9920-9924. [PDF]
2. G.F. Schröder and H. Grubmüller. FRETsg : Biomolecular structure model building from multiple FRET experiments.
Comp. Phys. Comm. (2003) 158:150-157. [PDF]
1. G.F. Schröder Molekulardynamiksimulation der Flexibilität und Fluoreszenzanisotropie eines an ein Protein gebundenen Farbstoffs, Diploma Thesis, Universität Göttingen, 2001. [PDF]