Open access to cutting-edge electron and light microscopy
We provide researchers from Europe and beyond with a synergistic portfolio of imaging services including cryo-EM, super-resolution and intravital microscopy to enable new ground-breaking research that crosses the scales of biology.
Some of the user stories and publications listed are based on the successful interim service operation in cryo-electron microscopy by EMBL’s cryo-EM platform.
However in September 2021 we welcomed our first onsite user Pia Lavriha who came to use our correlative microscopy services. Read more.
ETH Zurich and Paul Scherrer Institute, Switzerland
In October 2021 we welcomed our first onsite pilot user for light microscopy services – Danny Ionescu: “For me, it was a fantastic experience, both from a technological and scientific aspect but also due to the engagement of the Imaging Centre team who made all efforts to address my research needs and provide methods specifically tailored for my unique samples.”
Leibniz Institute of Freshwater Ecology and Inland Fisheries, Germany
Weizmann Institute of Science, Israel
“If there’s a possibility to get scope time in Heidelberg, that would be a better choice than any other microscope in the world today, just because of the little tweaks they made. We were able for the first time to determine the structure of FAS-1 multi-enzyme complex to high enough resolution to now try the approach to locate the drug bound to the complex.” Read more
Department of Biological Sciences, Birkbeck College, United Kingdom
“At EMBL we collected a dataset that we used to obtain a 4.9 Å structure of the assembled COPII coat, now published in Nature Communications. This is the highest-resolution structure of a membrane-assembled coat, and one of the highest-resolution subtomogram averages obtained so far.” Read more
Institute of Biochemistry, ETH Zurich, Switzerland
“Using the data collected at EMBL, we were able to reconstruct the 3D structure of the membrane adenylyl cyclase AC9 bound to a G protein alpha subunit at 3.4 Å resolution and publish it in Science in April 2019.” Read more
Institute of Genetics and Molecular and Cellular Biology, France
“The resolution of data we collected at EMBL was high enough to visualise the bound substrate in the active site, and a single dataset allowed us to directly visualise two mutually exclusive states – the reactivated, substrate-bound state of RNA polymerase and the Gre factor-bound state.” Read more
Institute of Protein Biochemistry, Ulm University, Germany
“The samples I’m working with are often unevenly distributed on a grid and in the holes. Wim Hagen from EMBL Cryo-EM platform helped find a solution to manually pick the sample in an efficient way with SerialEM and get good results for two Nature Communications papers.” Read more
University College Cork, Ireland
“Although we did not succeed in capturing the structure of the ribosome primed for bypassing of MGS13 mRNA, we did determine the structure of the bacterial ribosome at an unprecedented resolution of 1.55 Å thanks to the incredible facilities available at the EMBL Imaging Centre and the fantastic work carried out by Simon Fromm.” Read more
Electron Microscopy Facility of IIT, Italy
“All the experiments, both grid screening and high-end data collections, have been performed virtually due to the COVID-19 pandemic. Nevertheless, Dr. Simone Mattei was really helpful in evaluating our results. We could participate in remote and assist Dr. Simon Fromm in the various stages of sample screening and data collection. This experience was very helpful and instructive.” Read more
University of Utrecht, the Netherlands
“Thanks to the use of MINFLUX, we could obtain data on the localization of the full-length CSPP1, as well as its fragments. Before the development of the MINFLUX technology, it was not possible to determine whether the protein localises on the inside or outside of microtubules, least of all individual protein domains.” Read more
Gritti N, Power RM, Graves A, Huisken J. (2024)
Image restoration of degraded time-lapse microscopy data mediated by near-infrared imaging. Nat Methods. doi: https://doi.org/10.1038/s41592-023-02127-z
Gemin O, Armijo V, Hons M, Bissardon C, Linares R, Bowler MW, Wolff G, Kovalev K, Babenko A, Salo VT, Schneider S, Rossi C, Lecomte L, Deckers T, Lauzier K, Janocha R, Felisaz F, Sinoir J, Galej W, Mahamid J, Müller CW, Eustermann S, Mattei S, Cipriani F, Papp G. (2024)
EasyGrid: A versatile platform for automated cryo-EM sample preparation and quality control. bioRxiv 2024.01.18.576170; doi: https://doi.org/10.1101/2024.01.18.576170
Torres-Sánchez L, Géry Sana T, Decossas M, Hashem Y, Krasteva PV. (2023)
Structures of the P. aeruginosa FleQ-FleN master regulators reveal large-scale conformational switching in motility and biofilm control. Proc Natl Acad Sci U S A. 2023 Dec 12;120(50):e2312276120. doi: 10.1073/pnas.2312276120.
Hennies J, Serra Lleti JM, Pape C, Bekbayev S, Gross V, Kreshuk A, Schwab Y. (2023)
CebraEM: A practical workflow to segment cellular organelles in volume SEM datasets using a transferable CNN-based membrane prediction. bioRxiv 2023.04.06.535829; doi: https://doi.org/10.1101/2023.04.06.535829
Power RM, Tschanz A, Zimmermann T, Ries J. (2023)
Automated 3D multi-color single-molecule localization microscopy. bioRxiv 2023.10.23.563122; doi: https://doi.org/10.1101/2023.10.23.563122
Adamoski D, Dias MM, Quesñay JEN, Yang Z, Zagoriy I, Steyer AM, Rodrigues CT, da Silva Bastos AC, da Silva BN, Costa RKE, de Abreu FMO, Islam Z, Cassago A, van Heel MG, Consonni SR, Mattei S, Mahamid J, Portugal RV, Ambrosio ALB, Dias SMG. (2023)
Molecular mechanism of glutaminase activation through filamentation and the role of filaments in mitophagy protection. Nat Struct Mol Biol. 2023 Oct 19. doi: 10.1038/s41594-023-01118-0.
Caspy I, Fadeeva M, Mazor Y, Nelson N. (2023)
Structure of Dunaliella photosystem II reveals conformational flexibility of stacked and unstacked supercomplexes. Elife. 2023 Feb 17;12:e81150. doi: 10.7554/eLife.81150.
Fadeeva M, Klaiman D, Caspy I, Nelson N. (2023)
Structure of Chlorella ohadii Photosystem II Reveals Protective Mechanisms against Environmental Stress. Cells. 2023 Jul 31;12(15):1971. doi: 10.3390/cells12151971.
Heerde T, Bansal A, Schmidt M, Fändrich M. (2023)
Cryo-EM structure of a catalytic amyloid fibril. Sci Rep. 2023 Mar 11;13(1):4070. doi: 10.1038/s41598-023-30711-y.
Heerde T, Schütz D, Lin YJ, Münch J, Schmidt M, Fändrich M. (2023)
Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril. Nat Commun. 2023 Jul 18;14(1):4293. doi: 10.1038/s41467-023-40042-1.
Sharma K, Banerjee S, Savran D, Rajes C, Wiese S, Girdhar A, Schwierz N, Lee C, Shorter J, Schmidt M, Guo L, Fändrich M. (2023)
Cryo-EM Structure of the Full-length hnRNPA1 Amyloid Fibril. J Mol Biol. 2023 Sep 15;435(18):168211. doi: 10.1016/j.jmb.2023.168211.
Prevost MS, Barilone N, Dejean de la Bâtie G, Pons S, Ayme G, England P, Gielen M, Bontems F, Pehau-Arnaudet G, Maskos U, Lafaye P, Corringer PJ. (2023)
An original potentiating mechanism revealed by the cryo-EM structures of the human α7 nicotinic receptor in complex with nanobodies. Nat Commun. 2023 Sep 25;14(1):5964. doi: 10.1038/s41467-023-41734-4.
Juyoux P, Galdadas I, Gobbo D, von Velsen J, Pelosse M, Tully M, Vadas O, Gervasio FL, Pellegrini E, Bowler MW. (2023)
Architecture of the MKK6-p38α complex defines the basis of MAPK specificity and activation. Science. 2023 Sep 15;381(6663):1217-1225. doi: 10.1126/science.add7859.
Fromm SA, O’Connor KM, Purdy M, Bhatt PR, Loughran G, Atkins JF, Jomaa A, Mattei S. (2023)
The translating bacterial ribosome at 1.55 Å resolution generated by cryo-EM imaging services. Nat Commun. 2023 Feb 25;14(1):1095. doi: 10.1038/s41467-023-36742-3.
Ganeva I, Lim K, Boulanger J, Hoffmann PC, Muriel O, Borgeaud AC, Hagen WJH, Savage DB, Kukulski W. (2023)
The architecture of Cidec-mediated interfaces between lipid droplets. Cell Rep. 2023 Feb 15;42(2):112107. doi: 10.1016/j.celrep.2023.112107.
van den Berg CM, Volkov VA, Schnorrenberg S, Huang Z, Stecker KE, Grigoriev I, Gilani S, Frikstad KM, Patzke S, Zimmermann T, Dogterom M, Akhmanova A. (2023)
CSPP1 stabilizes growing microtubule ends and damaged lattices from the luminal side. J Cell Biol. 2023 Apr 3;222(4):e202208062. doi: 10.1083/jcb.202208062.
Kalbermatter D, Jeckelmann JM, Wyss M, Shrestha N, Pliatsika D, Riedl R, Lemmin T, Plattet P, Fotiadis D. (2023)
Structure and supramolecular organization of the canine distemper virus attachment glycoprotein. Proc Natl Acad Sci U S A. 2023 Feb 7;120(6):e2208866120. doi: 10.1073/pnas.2208866120.
Prouteau M, Bourgoint C, Felix J, Bonadei L, Sadian Y, Gabus C, Savvides SN, Gutsche I, Desfosses A, Loewith R. (2023)
EGOC inhibits TOROID polymerization by structurally activating TORC1. Nat Struct Mol Biol. 2023 Jan 26. doi: 10.1038/s41594-022-00912-6.
Dolce LG, Zimmer AA, Tengo L, Weis F, Rubio MAT, Alfonzo JD, Kowalinski E. (2022)
Structural basis for sequence-independent substrate selection by eukaryotic wobble base tRNA deaminase ADAT2/3. Nat Commun. 2022 Nov 8;13(1):6737. doi: 10.1038/s41467-022-34441-z.
Förderer A, Li E, Lawson AW, Deng YN, Sun Y, Logemann E, Zhang X, Wen J, Han Z, Chang J, Chen Y, Schulze-Lefert P, Chai J. (2022)
A wheat resistosome defines common principles of immune receptor channels. Nature. 2022 Oct;610(7932):532-539. doi: 10.1038/s41586-022-05231-w.
Huber ST, Sarajlic E, Huijink R, Weis F, Evers WH, Jakobi AJ. (2022)
Nanofluidic chips for cryo-EM structure determination from picoliter sample volumes. Elife. 2022 Jan 21;11:e72629. doi: 10.7554/eLife.72629.
Steinebrei M, Gottwald J, Baur J, Röcken C, Hegenbart U, Schönland S, Schmidt M. (2022)
Cryo-EM structure of an ATTRwt amyloid fibril from systemic non-hereditary transthyretin amyloidosis. Nat Commun. 2022 Oct 27;13(1):6398. doi: 10.1038/s41467-022-33591-4.
Martinez-Molledo M, Nji E, Reyes N. (2022)
Structural insights into the lysophospholipid brain uptake mechanism and its inhibition by syncytin-2. Nat Struct Mol Biol. 2022 Jun;29(6):604-612. doi: 10.1038/s41594-022-00786-8.
Fung HKH, Hayashi Y, Salo VT, Babenko A, Zagoriy I, Brunner A, Ellenberg J, Müller CW, Cuylen-Haering S, Mahamid J.
Genetically encoded multimeric tags for intracellular protein localisation in cryo-EM. bioRxiv 2022.12.10.519870; doi: https://doi.org/10.1101/2022.12.10.519870
Banerjee S, Baur J, Daniel C, Pfeiffer PB, Hitzenberger M, Kuhn L, Wiese S, Bijzet J, Haupt C, Amann KU, Zacharias M, Hazenberg BPC, Westermark GT, Schmidt M, Fändrich M. (2022)
Amyloid fibril structure from the vascular variant of systemic AA amyloidosis. Nat Commun. 2022 Nov 25;13(1):7261. doi: 10.1038/s41467-022-34636-4.
Fromm SA, O’Connor KM, Purdy M, Bhatt PR, Loughran G, Atkins JF, Jomaa A, Mattei S. (2022)
The translating bacterial ribosome at 1.55 Å resolution by open access cryo-EM. bioRxiv 2022.08.30.505838; doi: https://doi.org/10.1101/2022.08.30.505838
Deguchi T, Iwanski MK, Schentarra E, Heidebrecht C, Schmidt L, Heck J, Weihs T, Schnorrenberg S, Hoess P, Liu S, Chevyreva V, Noh K, Kapitein LC, Ries J.
Direct observation of motor protein stepping in living cells using MINFLUX. (2022) bioRxiv 2022.07.25.500391; doi: https://doi.org/10.1101/2022.07.25.500391
Čavka I, Power RM, Walsh D, Zimmermann T, Köhler S. (2022)
Super-Resolution Microscopy of the Synaptonemal Complex within the Caenorhabditis elegans Germline. J Vis Exp. 2022 Sep 13;(187). doi: 10.3791/64363.
Jeckelmann JM, Lemmin T, Schlapschy M, Skerra A, Fotiadis D. (2022)
Structure of the human heterodimeric transporter 4F2hc-LAT2 in complex with Anticalin, an alternative binding protein for applications in single-particle cryo-EM. Sci Rep. 2022 Oct 30;12(1):18269. doi: 10.1038/s41598-022-23270-1.
Lenarčič T, Niemann M, Ramrath DJF, Calderaro S, Flügel T, Saurer M, Leibundgut M, Boehringer D, Prange C, Horn EK, Schneider A, Ban N. (2022)
Mitoribosomal small subunit maturation involves formation of initiation-like complexes. Proc Natl Acad Sci U S A. 2022 Jan 18;119(3):e2114710118. doi: 10.1073/pnas.2114710118.
Zhu C, Guo X, Dumas P, Takacs M, Abdelkareem M, Vanden Broeck A, Saint-André C, Papai G, Crucifix C, Ortiz J, Weixlbaumer A. (2022)
Transcription factors modulate RNA polymerase conformational equilibrium. Nat Commun. 2022 Mar 22;13(1):1546. doi: 10.1038/s41467-022-29148-0.
Baudin F, Murciano B, Fung HKH, Fromm SA, Mattei S, Mahamid J, Müller CW. (2022)
Mechanism of RNA polymerase I selection by transcription factor UAF. Sci Adv. 2022 Apr 22;8(16):eabn5725. doi: 10.1126/sciadv.abn5725.
Arragain B, Durieux Trouilleton Q, Baudin F, Provaznik J, Azevedo N, Cusack S, Schoehn G, Malet H. (2022) Structural snapshots of La Crosse virus polymerase reveal the mechanisms underlying Peribunyaviridae replication and transcription. Nat Commun. 2022 Feb 16;13(1):902. doi: 10.1038/s41467-022-28428-z.
Itoh Y, Khawaja A, Laptev I, Cipullo M, Atanassov I, Sergiev P, Rorbach J, Amunts A. (2022)
Mechanism of mitoribosomal small subunit biogenesis and preinitiation. Nature. 2022 Jun;606(7914):603-608. doi: 10.1038/s41586-022-04795-x.
Goutam K, Ielasi FS, Pardon E, Steyaert J, Reyes N. (2022)
Structural basis of sodium-dependent bile salt uptake into the liver. Nature. 2022 Jun;606(7916):1015-1020. doi: 10.1038/s41586-022-04723-z.
Saridakis E, Vishwakarma R, Lai-Kee-Him J, Martin K, Simon I, Cohen-Gonsaud M, Coste F, Bron P, Margeat E, Boudvillain M. (2022)
Cryo-EM structure of transcription termination factor Rho from Mycobacterium tuberculosis reveals bicyclomycin resistance mechanism.
Commun Biol. 2022 Feb 9;5(1):120. https://doi.org/10.1038/s42003-022-03069-6.
Hochheiser IV, Pilsl M, Hagelueken G, Moecking J, Marleaux M, Brinkschulte R, Latz E, Engel C, Geyer M. (2022)
Structure of the NLRP3 decamer bound to the cytokine release inhibitor CRID3.
Nature. 2022 Feb 3. https://doi.org/10.1038/s41586-022-04467-w.
Heerde T, Rennegarbe M, Biedermann A, Savran D, Pfeiffer PB, Hitzenberger M, Baur J, Puscalau-Girtu I, Zacharias M, Schwierz N, Haupt C, Schmidt M, Fändrich M. (2022)
Cryo-EM demonstrates the in vitro proliferation of an ex vivo amyloid fibril morphology by seeding.
Nat Commun 13, 85. doi: 10.1038/s41467-021-27688-5.
Kišonaitė M, Wild K, Lapouge K, Ruppert T, Sinning I. (2022)
High-resolution structures of a thermophilic eukaryotic 80S ribosome reveal atomistic details of translocation.
Nat Commun 13, 476. https://doi.org/10.1038/s41467-022-27967-9.
Kadan Y, Tollervey F, Varsano N, Mahamid J, Gal A. (2021)
Intracellular nanoscale architecture as a master regulator of calcium carbonate crystallization in marine microalgae. Proc Natl Acad Sci U S A. 2021 Nov 16;118(46):e2025670118. doi: 10.1073/pnas.2025670118.
Andriko von Kügelgen, Vikram Alva, Tanmay A.M. Bharat (2021)
Complete atomic structure of a native archaeal cell surface
Cell Reports https://doi.org/10.1016/j.celrep.2021.110052
Ru Ta Gerasimaitė, Jonas Bucevičius, Kamila A Kiszka, Sebastian Schnorrenberg, Georgij Kostiuk, Tanja Koenen, Gražvydas Lukinavičius (2021)
Blinking Fluorescent Probes for Tubulin Nanoscopy in Living and Fixed Cells
ACS Chem Biol https://pubs.acs.org/doi/10.1021/acschembio.1c00538
Qin Yu, Alba Herrero del Valle, Rahul Singh, Yorgo Modis (2021)
MDA5 disease variant M854K prevents ATP-dependent structural discrimination of viral and cellular RNA
Nat Communications https://doi.org/10.1038/s41467-021-27062-5
Irma Querques, Michael Schmitz, Seraina Oberli, Christelle Chanez, Martin Jinek (2021)
Target site selection and remodelling by type V CRISPR-transposon systems
Nature https://doi.org/10.1038/s41586-021-04030-z
Juan C Canul-Tec, Anand Kumar, Jonathan Dhenin, Reda Assal, Pierre Legrand, Martial Rey, Julia Chamot-Rooke, Nicolas Reyes (2021)
The ion-coupling mechanism of human excitatory amino acid transporters
EMBO J https://doi.org/10.15252/embj.2021108341
Lynn Radamaker, Sara Karimi-Farsijani, Giada Andreotti, Julian Baur, Matthias Neumann, Sarah Schreiner, Natalie Berghaus, Raoul Motika, Christian Haupt, Paul Walther, Volker Schmidt, Stefanie Huhn, Ute Hegenbart, Stefan O. Schönland, Sebastian Wiese, Clarissa Read, Matthias Schmidt & Marcus Fändrich (2021)
Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM
Nat Communications https://doi.org/10.1038/s41467-021-26553-9
Ido Caspy, Ehud Neumann, Maria Fadeeva, Varda Liveanu, Anton Savitsky, Anna Frank, Yael Levi Kalisman, Yoel Shkolnisky, Omer Murik, Haim Treves, Volker Hartmann, Marc M. Nowaczyk, Wolfgang Schuhmann, Matthias Rögner, Itamar Willner, Aaron Kaplan, Gadi Schuster, Nathan Nelson, Wolfgang Lubitz, Rachel Nechushtai (2021)
Cryo-EM photosystem I structure reveals adaptation mechanisms to extreme high light in Chlorella ohadii
Nat Plants https://doi.org/10.1038/s41477-021-00983-1
Charlotte Guyomar, Gaetano D’Urso, Sophie Chat, Emmanuel Giudice, Reynald Gillet (2021)
Structures of tmRNA and SmpB as they transit through the ribosome
Nat Commun 12, 4909 https://doi.org/10.1038/s41467-021-24881-4
Stephan Hirschi, David Kalbermatter, Zöhre Ucurum, Thomas Lemmin, Dimitrios Fotiadis (2021)
Cryo-EM structure and dynamics of the green-light absorbing proteorhodopsin
Nat Commun 12, 4107 https://doi.org/10.1038/s41467-021-24429-6
Julien Bous, Hélène Orcel, Nicolas Floquet, Cédric Leyrat, Joséphine Lai-Kee-Him, Gérald Gaibelet, Aurélie Ancelin, Julie Saint-Paul, Stefano Trapani, Maxime Louet, Rémy Sounier, Hélène Déméné, Sébastien Granier, Patrick Bron, Bernard Mouillac (2021)
Cryo-electron microscopy structure of the antidiuretic hormone arginine-vasopressin V2 receptor signaling complex
Sci Adv. 7(21):eabg5628. doi: 10.1126/sciadv.abg5628
Martin Obr, Clifton L Ricana, Nadia Nikulin, Jon-Philip R Feathers, Marco Klanschnig, Andreas Thader, Marc C Johnson, Volker M Vogt, Florian K M Schur, Robert A Dick (2021)
Structure of the mature Rous sarcoma virus lattice reveals a role for IP6 in the formation of the capsid hexamer
Nat Commun 12 (1), 3226. doi: 10.1038/s41467-021-23506-0
Joshua Hutchings, Viktoriya G. Stancheva, Nick R. Brown, Alan C. M. Cheung, Elizabeth A. Miller, Giulia Zanetti (2021)
Structure of the complete, membrane-assembled COPII coat reveals a complex interaction network
Nat Commun 12, 2034. https://doi.org/10.1038/s41467-021-22110-6
Laura Plassart, Ramtin Shayan, Christian Montellese, Dana Rinaldi, Natacha Larburu, Carole Pichereaux, Carine Froment, Simon Lebaron, Marie-Françoise O’Donohue, Ulrike Kutay, Julien Marcoux, Pierre-Emmanuel Gleizes, Celia Plisson-Chastang (2021)
The final step of 40S ribosomal subunit maturation is controlled by a dual key lock
eLife 2021;10:e61254 doi: 10.7554/eLife.61254
Bansal A, Schmidt M, Rennegarbe M, Haupt C, Liberta F, Stecher S, Puscalau-Girtu I, Biedermann A, Fändrich M. (2021)
AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils
Nat Commun. 12(1):1013. doi: 10.1038/s41467-021-21129-z
Radamaker L, Baur J, Huhn S, Haupt C, Hegenbart U, Schönland S, Bansal A, Schmidt M, Fändrich M. (2021)
Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis
Nat Commun. 12(1):875. doi: 10.1038/s41467-021-21126-2
Yu Q, Herrero del Valle A, Singh R, Modis Y. (2021)
MDA5 autoimmune disease variant M854K prevents ATP-dependent structural discrimination of viral and cellular RNA
bioRxiv. doi.org/10.1101/2021.02.01.429133
Kraushar ML, Krupp F, Harnett D, Turko P, Ambrozkiewicz MC, Sprink T, Imami K, Günnigmann M, Zinnall U, Vieira-Vieira CH, Schaub T, Münster-Wandowski A, Bürger J, Borisova E, Yamamoto H, Rasin MR, Ohler U, Beule D, Mielke T, Tarabykin V, Landthaler M, Kramer G, Vida I, Selbach M, Spahn CMT. (2021)
Protein Synthesis in the Developing Neocortex at Near-Atomic Resolution Reveals Ebp1-Mediated Neuronal Proteostasis at the 60S Tunnel Exit
Mol Cell. 2021 Jan 21;81(2):304-322.e16. doi.org/10.1016/j.molcel.2020.11.037
McDowell MA, Heimes M, Fiorentino F, Mehmood S, Farkas Á, Coy-Vergara J, Wu D, Bolla JR, Schmid V, Heinze R, Wild K, Flemming D, Pfeffer S, Schwappach B, Robinson CV, Sinning I. (2020)
Structural Basis of Tail-Anchored Membrane Protein Biogenesis by the GET Insertase Complex
Mol Cell. 2020 Oct 1;80(1):72-86.e7. doi: 10.1016/j.molcel.2020.08.012.
Kumar A, Planchais C, Fronzes R, Mouquet H, Reyes N (2020)
Binding mechanisms of therapeutic antibodies to human CD20
Science, Vol. 369, Issue 6505, pp. 793-799. doi.org/10.1126/science.abb8008
Ahel J, Lehner A, Vogel A, Schleiffer A, Meinhart A, Haselbach D, Clausen T. (2020)
Moyamoya disease factor RNF213 is a giant E3 ligase with a dynein-like core and a distinct ubiquitin-transfer mechanism
eLife. doi.org/10.7554/eLife.56185
Moser von Filseck J, Barberi L, Talledge N, Johnson IE, Frost A, Lenz M, Roux A. (2020)
Anisotropic ESCRT-III architecture governs helical membrane tube formation
Nat Commun 11, 1516. doi.org/10.1038/s41467-020-15327-4
Bertin A, de Franceschi N, de la Mora E, Maiti S, Alqabandi M, Miguet N, di Cicco A, Roos W, Mangenot S, Weissenhorn W, Bassereau P. (2020)
Human ESCRT-III polymers assemble on positively curved membranes and induce helical membrane tube formation
Nat Commun 11, 2663. doi.org/10.1038/s41467-020-16368-5
Flaugnatti N, Rapisarda C , Rey M, Beauvois SG, Nguyen VA, Canaan S, Durand E, Chamot‐Rooke J, Cascales E, Fronzes R, Journet L. (2020)
Structural basis for loading and inhibition of a bacterial T6SS phospholipase effector by the VgrG spike
The EMBO Journal 39: 39: e104129, doi.org/10.15252/embj.2019104129
Cannac F, Qi C, Falschlunger J, Hausmann G, Basler K, Korkhov VM. (2020)
Cryo-EM structure of the Hedgehog release protein Dispatched
Science Advances, Vol 6:16, doi.org/10.1126/sciadv.aay7928
Von Kügelgen A, Tang H, Hardy GG, Kureisaite-Ciziene D, Brun YV, Stansfeld PJ, Robinson CV, Bharat TAM (2020)
In Situ Structure of an Intact Lipopolysaccharide-Bound Bacterial Surface Layer
Cell. 180 (2): 348-358, doi: https://doi.org/10.1016/j.cell.2019.12.006
Webster MW, Takacs M, Zhu C, Vidmar V, Eduljee A, Abdelkareem M, Weixlbaumer A. (2020)
Structural basis of transcription-translation coupling and collision in bacteria
Science, Vol. 369, Issue 6509, pp. 1355-1359. doi: 10.1126/science.abb5036
Kollmer M, Close W, Funk L, Rasmussen J, Bsoul A, Schierhorn A, Schmidt M, Sigurdson CJ, Jucker M, Fändrich M. (2019)
Cryo-EM structure and polymorphism of Aβamyloid fibrils purified from Alzheimer’s brain tissue
Nat Commun. 10(1):4760. doi: 10.1038/s41467-019-12683-8
Schmidt M, Wiese S, Adak V, Engler J, Agarwal S, Fritz G, Westermark P, Zacharias M, Fändrich M. (2019)
Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis
Nat Commun. 10(1): 5008. doi: 10.1038/s41467-019-13038-z
Abdelkareem M, Saint-André C, Takacs M, Papai G, Crucifix C, Guo X, Ortiz J, Weixlbaumer A. (2019)
Structural Basis of Transcription: RNA Polymerase Backtracking and Its Reactivation
Mol Cell. S1097-2765(19)30321-1 doi: 10.1016/j.molcel.2019.04.029
Qi C, Sorrentino S, Medalia O, Korkhov VM. (2019)
The structure of a membrane adenylyl cyclase bound to an activated stimulatory G protein
Science 364(6438): 389-394 doi: 10.1126/science.aav0778
Radamaker L, Lin YH, Annamalai K, Huhn S, Hegenbart U, Schönland SO, Fritz G, Schmidt M, Fändrich M. (2019)
Cryo-EM structure of a light chain-derived amyloid fibril from a patient with systemic AL amyloidosis.
Nat Commun. 10 (1):1103 doi: 10.1038/s41467-019-09032-0
Liberta F, Loerch S, Rennegarbe M, Schierhorn A, Westermark P, Westermark GT, Hazenberg BPC, Grigorieff N, Fändrich M, Schmidt M. (2019)
Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids
Nat Commun. 10 (1):1104. doi:10.1038/s41467-019-09033-z
Cuervo A, Fàbrega-Ferrer M, Machón C, Conesa JJ, Fernández FJ, Pérez-Luque R, Pérez-Ruiz M, Pous J, Vega CM, Carrascosa JL, Coll M. (2019)
Structures of T7 bacteriophage portal and tail suggest a viral DNA retention and ejection mechanism
Nat Commun. 10: 3746. doi: 10.1038/s41467-019-11705-9
Qi C, Di Minin G, Vercellino I, Wutz A, Korkhov VM (2019)
Structural basis of sterol recognition by human hedgehog receptor PTCH1
Sci Adv. 2019 Sep; 5(9): eaaw6490. doi: 10.1126/sciadv.aaw6490
Desfosses A, Venugopal H, Joshi T, Felix J, Jessop M, Jeong H, Hyun J, Heymann JB, Hurst MRH, Gutsche I, Mitra AK (2019)
Atomic structures of an entire contractile injection system in both the extended and contracted states
Nature Microbiology. doi 10.1038/s41564-019-0530-6
Krupp F, Said N, Huang YH, Loll B, Bürger J, Mielke T, Spahn CMT, Wahl MC. (2019)
Structural Basis for the Action of an All-Purpose Transcription Anti-termination Factor
Molecular Cell, 74:1, 143-157. doi: 10.1016/j.molcel.2019.01.016
Oosterheert W, van Bezouwen LS, Rodenburg RNP, Granneman J, Förster F, Mattevi A, Gros P. (2018)
Cryo-EM structures of human STEAP4 reveal mechanism of iron(III) reduction.
Nat Commun. 9(1):4337. doi: 10.1038/s41467-018-06817-7
Hutchings J, Stancheva V, Miller EA, Zanetti G. (2018)
Subtomogram averaging of COPII assemblies reveals how coat organization dictates membrane shape.
Nat Commun. 9(1):4154. doi: 10.1038/s41467-018-06577-4
Abascal-Palacios G, Ramsay EP, Beuron F, Morris E, Vannini A. (2018)
Structural basis of RNA polymerase III transcription initiation.
Nature 553(7688):301-306. doi: 10.1038/nature25441
Elad, N, Baron S, Peleg Y, Albeck S, Grunwald J, Raviv G, Shakked Z, Zimhony O, Diskin R (2018)
Structure of Type-I Mycobacterium tuberculosis fatty acid synthase at 3.3 Å resolution
Molecular Cell, 74:1. doi: 10.1016/j.molcel.2019.01.016
Böttcher B, Nassal M. (2018)
Structure of Mutant Hepatitis B Core Protein Capsids with Premature Secretion Phenotype
JMB, 430:24. doi: 10.1016/j.jmb.2018.10.018