Cutting-edge electron and light microscopy technologies
The publications listed so far are based on the EMBL Cryo-EM Service Platform.
Total: 37 publications
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
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
Hutchings J, Stancheva VG, Brown NR, Cheung AMC, Miller E, Zanetti G. (2020)
Structure of the complete, membrane-assembled COPII coat reveals a complex interaction network
bioRxiv. doi.org/10.1101/2020.06.18.159608
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
Wandzik JM, Kouba T, Karuppasamy M, Pflug A, Drncova P, Provaznik J, Azevedo N, Cusack S. (2020)
A Structure-Based Model for the Complete Transcription Cycle of Influenza Polymerase
Cell.. 181: 1-17. doi: 10.1016/j.cell.2020.03.061
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
Weis F, Menting JG, Margetts MB, Chan SJ, Xu Y, Tennagels N, Wohlfart P, Langer T, Müller CW, Dreyer MK, Lawrence MC. (2018)
The signalling conformation of the insulin receptor ectodomain.
Nat Commun. 9(1):4420. doi: 10.1038/s41467-018-06826-6
Zivanov J, Nakane T, Forsberg BO, Kimanius D, Hagen WJ, Lindahl E, Scheres SH. (2018)
New tools for automated high-resolution cryo-EM structure determination in RELION-3.
Elife. 7. pii: e42166. doi: 10.7554/eLife.42166
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
Vorländer MK, Khatter H, Wetzel R, Hagen WJH, Müller CW. (2018)
Molecular mechanism of promoter opening by RNA polymerase III.
Nature 553(7688):295-300. doi: 10.1038/nature25440
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
Sadian Y, Tafur L, Kosinski J, Jakobi AJ, Wetzel R, Buczak K, Hagen WJ, Beck M, Sachse C, Müller CW. (2017)
Structural insights into transcription initiation by yeast RNA polymerase I.
EMBO J. 36(18):2698-2709. doi: 10.15252/embj.201796958
Alewijnse B, Ashton AW, Chambers MG, Chen S, Cheng A, Ebrahim M, Eng ET, Hagen WJH, Koster AJ, López CS, Lukoyanova N, Ortega J, Renault L, Reyntjens S, Rice WJ, Scapin G, Schrijver R, Siebert A, Stagg SM, Grum-Tokars V, Wright ER, Wu S, Yu Z, Zhou ZH, Carragher B, Potter CS. (2017)
Best practices for managing large CryoEM facilities.
J Struct Biol. 199(3):225-236. doi: 10.1016/j.jsb.2017.07.011
Hagen WJH1, Wan W1, Briggs JAG2. (2017)
Implementation of a cryo-electron tomography tilt-scheme optimized for high resolution subtomogram averaging.
J Struct Biol. 197(2):191-198. doi: 10.1016/j.jsb.2016.06.007
Bharat TAM, Kureisaite-Ciziene D, Hardy GG, Yu EW, Devant JM, Hagen WJH, Brun YV, Briggs JAG, Löwe J. (2017)
Structure of the hexagonal surface layer on Caulobacter crescentus cells.
Nat Microbiol 2. doi: 10.1038/nmicrobiol.2017.59
Tafur L, Sadian Y, Hoffmann NA, Jakobi AJ, Wetzel R, Hagen WJ, Sachse C, Müller CW. (2016)
Molecular Structures of Transcribing RNA Polymerase I.
Mol Cell. 64(6):1135-1143. doi: 10.1016/j.molcel.2016.11.013
Mattei S, Glass B, Hagen WJ, Kräusslich HG, Briggs JA. (2016)
The structure and flexibility of conical HIV-1 capsids determined within intact virions.
Science 354(6318):1434-1437. doi: 10.1126/science.aah4972
Kosinski J, Mosalaganti S, von Appen A, Teimer R, DiGuilio AL, Wan W, Bui KH, Hagen WJ, Briggs JA, Glavy JS, Hurt E, Beck M. (2016)
Molecular architecture of the inner ring scaffold of the human nuclear pore complex.
Science 352(6283):363-365. doi: 10.1126/science.aaf0643
Schur FK, Obr M, Hagen WJ, Wan W, Jakobi AJ, Kirkpatrick JM, Sachse C, Kräusslich HG, Briggs JA. (2016)
An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation.
Science 353(6298):506-508. doi: 10.1126/science.aaf9620
Bertipaglia C, Schneider S, Jakobi AJ, Tarafder AK, Bykov YS, Picco A, Kukulski W, Kosinski J, Hagen WJ, Ravichandran AC, Wilmanns M, Kaksonen M, Briggs JA, 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. doi: 10.15252/embr.201541960