Balzarotti, Francisco

[["dc.bibliographiccitation.artnumber","527a"],["dc.bibliographiccitation.issue","6285"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.volume","352"],["dc.contributor.author","Sahl, Steffen J."],["dc.contributor.author","Balzarotti, Francisco"],["dc.contributor.author","Keller-Findeisen, Jan"],["dc.contributor.author","Leutenegger, Marcel"],["dc.contributor.author","Westphal, Volker"],["dc.contributor.author","Egner, Alexander"],["dc.contributor.author","Lavoie-Cardinal, Flavie"],["dc.contributor.author","Chmyrov, Andriy"],["dc.contributor.author","Grotjohann, Tim"],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:54:33Z"],["dc.date.available","2017-09-07T11:54:33Z"],["dc.date.issued","2016"],["dc.description.abstract","Li et al. (Research Articles, 28 August 2015, aab3500) purport to present solutions to longstanding challenges in live-cell microscopy, reporting relatively fast acquisition times in conjunction with improved image resolution. We question the methods' reliability to visualize specimen features at sub-100-nanometer scales, because the mandatory mathematical processing of the recorded data leads to artifacts that are either difficult or impossible to disentangle from real features. We are also concerned about the chosen approach of subjectively comparing images from different super-resolution methods, as opposed to using quantitative measures."],["dc.identifier.doi","10.1126/science.aad7983"],["dc.identifier.gro","3141696"],["dc.identifier.isi","000374998600028"],["dc.identifier.pmid","27126030"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1095-9203"],["dc.relation.issn","0036-8075"],["dc.title","Comment on \"Extended-resolution structured illumination imaging of endocytic and cytoskeletal dynamics\""],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","606"],["dc.bibliographiccitation.issue","6325"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","612"],["dc.bibliographiccitation.volume","355"],["dc.contributor.author","Balzarotti, Francisco"],["dc.contributor.author","Eilers, Yvan"],["dc.contributor.author","Gwosch, Klaus C."],["dc.contributor.author","Gynnå, Arvid H."],["dc.contributor.author","Westphal, Volker"],["dc.contributor.author","Stefani, Fernando D."],["dc.contributor.author","Elf, Johan"],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2018-01-17T13:33:22Z"],["dc.date.available","2018-01-17T13:33:22Z"],["dc.date.issued","2017"],["dc.description.abstract","We introduce MINFLUX, a concept for localizing photon emitters in space. By probing the emitter with a local intensity minimum of excitation light, MINFLUX minimizes the fluorescence photons needed for high localization precision. In our experiments, 22 times fewer fluorescence photons are required as compared to popular centroid localization. In superresolution microscopy, MINFLUX attained ~1-nm precision, resolving molecules only 6 nanometers apart. MINFLUX tracking of single fluorescent proteins increased the temporal resolution and the number of localizations per trace by a factor of 100, as demonstrated with diffusing 30S ribosomal subunits in living Escherichia coli As conceptual limits have not been reached, we expect this localization modality to break new ground for observing the dynamics, distribution, and structure of macromolecules in living cells and beyond."],["dc.identifier.arxiv","1611.03401v1"],["dc.identifier.doi","10.1126/science.aak9913"],["dc.identifier.pmid","28008086"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11719"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1095-9203"],["dc.subject","Physics - Optics"],["dc.subject","Physics - Optics"],["dc.subject","Physics - Biological Physics"],["dc.title","Nanometer resolution imaging and tracking of fluorescent molecules with minimal photon fluxes"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.volume","39"],["dc.contributor.author","Stephan, Till"],["dc.contributor.author","Brüser, Christian"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Steyer, Anna M."],["dc.contributor.author","Balzarotti, Francisco"],["dc.contributor.author","Barbot, Mariam"],["dc.contributor.author","Behr, Tiana S."],["dc.contributor.author","Heim, Gudrun"],["dc.contributor.author","Hübner, Wolfgang"],["dc.contributor.author","Ilgen, Peter"],["dc.contributor.author","Lange, Felix"],["dc.contributor.author","Pacheu‐Grau, David"],["dc.contributor.author","Pape, Jasmin K."],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Huser, Thomas"],["dc.contributor.author","Hell, Stefan W."],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2021-04-14T08:25:12Z"],["dc.date.available","2021-04-14T08:25:12Z"],["dc.date.issued","2020"],["dc.description.abstract","Mitochondrial function is critically dependent on the folding of the mitochondrial inner membrane into cristae; indeed, numerous human diseases are associated with aberrant crista morphologies. With the MICOS complex, OPA1 and the F1Fo-ATP synthase, key players of cristae biogenesis have been identified, yet their interplay is poorly understood. Harnessing super-resolution light and 3D electron microscopy, we dissect the roles of these proteins in the formation of cristae in human mitochondria. We individually disrupted the genes of all seven MICOS subunits in human cells and re-expressed Mic10 or Mic60 in the respective knockout cell line. We demonstrate that assembly of the MICOS complex triggers remodeling of pre-existing unstructured cristae and de novo formation of crista junctions (CJs) on existing cristae. We show that the Mic60-subcomplex is sufficient for CJ formation, whereas the Mic10-subcomplex controls lamellar cristae biogenesis. OPA1 stabilizes tubular CJs and, along with the F1Fo-ATP synthase, fine-tunes the positioning of the MICOS complex and CJs. We propose a new model of cristae formation, involving the coordinated remodeling of an unstructured crista precursor into multiple lamellar cristae."],["dc.identifier.doi","10.15252/embj.2019104105"],["dc.identifier.pmid","32567732"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81550"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/51"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/115"],["dc.identifier.url","https://for2848.gwdguser.de/literature/publications/25"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P01: Untersuchung der Unterschiede in der Zusammensetzung, Funktion und Position von individuellen MICOS Komplexen in einzelnen Säugerzellen"],["dc.relation","SFB 1190 | P13: Protein Transport über den mitochondrialen Carrier Transportweg"],["dc.relation","FOR 2848: Architektur und Heterogenität der inneren mitochondrialen Membran auf der Nanoskala"],["dc.relation","FOR 2848 | P04: Analyse der räumlichen Organisation der OXPHOS Assemblierung in Säugerzellen"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.relation.workinggroup","RG Hell"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.relation.workinggroup","RG Möbius"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Riedel"],["dc.rights","CC BY 4.0"],["dc.title","MICOS assembly controls mitochondrial inner membrane remodeling and crista junction redistribution to mediate cristae formation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6117"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","6122"],["dc.bibliographiccitation.volume","115"],["dc.contributor.author","Eilers, Yvan"],["dc.contributor.author","Ta, Haisen"],["dc.contributor.author","Gwosch, Klaus C."],["dc.contributor.author","Balzarotti, Francisco"],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2022-03-01T11:46:24Z"],["dc.date.available","2022-03-01T11:46:24Z"],["dc.date.issued","2018"],["dc.description.abstract","Compared with localization schemes solely based on evaluating patterns of molecular emission, the recently introduced single-molecule localization concept called MINFLUX and the fluorescence nanoscopies derived from it require up to orders of magnitude fewer emissions to attain single-digit nanometer resolution. Here, we demonstrate that the lower number of required fluorescence photons enables MINFLUX to detect molecular movements of a few nanometers at a temporal sampling of well below 1 millisecond. Using fluorophores attached to thermally fluctuating DNA strands as model systems, we demonstrate that measurement times as short as 400 microseconds suffice to localize fluorescent molecules with ∼2-nm precision. Such performance is out of reach for popular camera-based localization by centroid calculation of emission diffraction patterns. Since theoretical limits have not been reached, our results show that emerging MINFLUX nanoscopy bears great potential for dissecting the motions of individual (macro)molecules at hitherto-unattained combinations of spatial and temporal resolution."],["dc.description.abstract","Compared with localization schemes solely based on evaluating patterns of molecular emission, the recently introduced single-molecule localization concept called MINFLUX and the fluorescence nanoscopies derived from it require up to orders of magnitude fewer emissions to attain single-digit nanometer resolution. Here, we demonstrate that the lower number of required fluorescence photons enables MINFLUX to detect molecular movements of a few nanometers at a temporal sampling of well below 1 millisecond. Using fluorophores attached to thermally fluctuating DNA strands as model systems, we demonstrate that measurement times as short as 400 microseconds suffice to localize fluorescent molecules with ∼2-nm precision. Such performance is out of reach for popular camera-based localization by centroid calculation of emission diffraction patterns. Since theoretical limits have not been reached, our results show that emerging MINFLUX nanoscopy bears great potential for dissecting the motions of individual (macro)molecules at hitherto-unattained combinations of spatial and temporal resolution."],["dc.identifier.doi","10.1073/pnas.1801672115"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103658"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1091-6490"],["dc.relation.issn","0027-8424"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0/"],["dc.title","MINFLUX monitors rapid molecular jumps with superior spatiotemporal resolution"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","103"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nano Letters"],["dc.bibliographiccitation.lastpage","106"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Testa, Ilaria"],["dc.contributor.author","D'Este, E."],["dc.contributor.author","Urban, Nicolai T."],["dc.contributor.author","Balzarotti, Francisco"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:44:46Z"],["dc.date.available","2017-09-07T11:44:46Z"],["dc.date.issued","2015"],["dc.description.abstract","We show that RESOLFT fluorescence nanoscopy, a low light level scanning superresolution technique employing reversibly switchable fluorescent proteins (rsFPs), is capable of dual-channel live-cell imaging that is virtually free of chromatic errors and temporal offsets. This is accomplished using rsEGFP and Dronpa, two rsFPs having similar spectra but different kinetics of switching and fluorescence emission. Our approach is demonstrated by imaging protein distributions and dynamics in living neurons and neuronal tissues."],["dc.identifier.doi","10.1021/nl503058k"],["dc.identifier.gro","3141985"],["dc.identifier.isi","000348086100017"],["dc.identifier.pmid","25423166"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3268"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1530-6992"],["dc.relation.issn","1530-6984"],["dc.title","Dual Channel RESOLFT Nanoscopy by Using Fluorescent State Kinetics"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","365102"],["dc.bibliographiccitation.issue","36"],["dc.bibliographiccitation.journal","Journal of Physics D: Applied Physics"],["dc.bibliographiccitation.volume","49"],["dc.contributor.author","Bordenave, Martin D."],["dc.contributor.author","Balzarotti, Francisco"],["dc.contributor.author","Stefani, Fernando D."],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2017-09-07T11:44:40Z"],["dc.date.available","2017-09-07T11:44:40Z"],["dc.date.issued","2016"],["dc.description.abstract","Commonly, in stimulated emission depletion (STED) fluorescence nanoscopy, light of a wavelength located at the red tail of the emission spectrum of the dye is used to shrink the effective fluorophore excitation volume and thus to obtain images with sub diffraction resolution. Here, we demonstrate that continuous wave (CW) STED nanoscopy is feasible using STED wavelengths located at the emission maximum, where the cross section for stimulated emission is up to 10-fold larger than at the red tail. As a result, STED imaging becomes possible at equally lower STED beam power. Besides, fluorophores that have been considered inapplicable in certain wavelength constellations are thus becoming usable."],["dc.identifier.doi","10.1088/0022-3727/49/36/365102"],["dc.identifier.gro","3141622"],["dc.identifier.isi","000384052800013"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2233"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Max Planck Society"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1361-6463"],["dc.relation.issn","0022-3727"],["dc.title","STED nanoscopy with wavelengths at the emission maximum"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","20607"],["dc.bibliographiccitation.issue","34"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","20614"],["dc.bibliographiccitation.volume","117"],["dc.contributor.author","Pape, Jasmin K."],["dc.contributor.author","Stephan, Till"],["dc.contributor.author","Balzarotti, Francisco"],["dc.contributor.author","Büchner, Rebecca"],["dc.contributor.author","Lange, Felix"],["dc.contributor.author","Riedel, Dietmar"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2021-04-14T08:24:20Z"],["dc.date.available","2021-04-14T08:24:20Z"],["dc.date.issued","2020"],["dc.description.abstract","The mitochondrial contact site and cristae organizing system (MICOS) is a multisubunit protein complex that is essential for the proper architecture of the mitochondrial inner membrane. MICOS plays a key role in establishing and maintaining crista junctions, tubular or slit-like structures that connect the cristae membrane with the inner boundary membrane, thereby ensuring a contiguous inner membrane. MICOS is enriched at crista junctions, but the detailed distribution of its subunits around crista junctions is unclear because such small length scales are inaccessible with established fluorescence microscopy. By targeting individually activated fluorophores with an excitation beam featuring a central zero-intensity point, the nanoscopy method called MINFLUX delivers single-digit nanometer-scale three-dimensional (3D) resolution and localization precision. We employed MINFLUX nanoscopy to investigate the submitochondrial localization of the core MICOS subunit Mic60 in relation to two other MICOS proteins, Mic10 and Mic19. We demonstrate that dual-color 3D MINFLUX nanoscopy is applicable to the imaging of organellar substructures, yielding a 3D localization precision of ∼5 nm in human mitochondria. This isotropic precision facilitated the development of an analysis framework that assigns localization clouds to individual molecules, thus eliminating a source of bias when drawing quantitative conclusions from single-molecule localization microscopy data. MINFLUX recordings of Mic60 indicate ringlike arrangements of multiple molecules with a diameter of 40 to 50 nm, suggesting that Mic60 surrounds individual crista junctions. Statistical analysis of dual-color MINFLUX images demonstrates that Mic19 is generally in close proximity to Mic60, whereas the spatial coordination of Mic10 with Mic60 is less regular, suggesting structural heterogeneity of MICOS."],["dc.identifier.doi","10.1073/pnas.2009364117"],["dc.identifier.pmid","32788360"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81251"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/61"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/124"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P01: Untersuchung der Unterschiede in der Zusammensetzung, Funktion und Position von individuellen MICOS Komplexen in einzelnen Säugerzellen"],["dc.relation.eissn","1091-6490"],["dc.relation.issn","0027-8424"],["dc.relation.workinggroup","RG Hell"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Multicolor 3D MINFLUX nanoscopy of mitochondrial MICOS proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","217"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Nature Methods"],["dc.bibliographiccitation.lastpage","224"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Gwosch, Klaus C."],["dc.contributor.author","Pape, Jasmin K."],["dc.contributor.author","Balzarotti, Francisco"],["dc.contributor.author","Hoess, Philipp"],["dc.contributor.author","Ellenberg, Jan"],["dc.contributor.author","Ries, Jonas"],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2022-03-01T11:46:02Z"],["dc.date.available","2022-03-01T11:46:02Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41592-019-0688-0"],["dc.identifier.pii","688"],["dc.identifier.pmid","31932776"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103535"],["dc.identifier.url","https://sfb1286.uni-goettingen.de/literature/publications/43"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation","SFB 1286: Quantitative Synaptologie"],["dc.relation","SFB 1286 | A07: Der Aufbau des synaptischen Cytoskeletts"],["dc.relation.eissn","1548-7105"],["dc.relation.issn","1548-7091"],["dc.relation.workinggroup","RG Hell"],["dc.rights.uri","http://www.springer.com/tdm"],["dc.title","MINFLUX nanoscopy delivers 3D multicolor nanometer resolution in cells"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","E191"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","E199"],["dc.bibliographiccitation.volume","114"],["dc.contributor.author","d'Este, E."],["dc.contributor.author","Kamin, D."],["dc.contributor.author","Balzarotti, F."],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2018-03-19T21:48:11Z"],["dc.date.available","2018-03-19T21:48:11Z"],["dc.date.issued","2016"],["dc.description.abstract","We used stimulated emission depletion (STED) superresolution microscopy to analyze the nanoscale organization of 12 glial and axonal proteins at the nodes of Ranvier of teased sciatic nerve fibers. Cytoskeletal proteins of the axon (betaIV spectrin, ankyrin G) exhibit a high degree of one-dimensional longitudinal order at nodal gaps. In contrast, axonal and glial nodal adhesion molecules [neurofascin-186, neuron glial-related cell adhesion molecule (NrCAM)] can arrange in a more complex, 2D hexagonal-like lattice but still feature a ∼190-nm periodicity. Such a lattice-like organization is also found for glial actin. Sodium and potassium channels exhibit a one-dimensional periodicity, with the Nav channels appearing to have a lower degree of organization. At paranodes, both axonal proteins (betaII spectrin, Caspr) and glial proteins (neurofascin-155, ankyrin B) form periodic quasi–one-dimensional arrangements, with a high degree of interdependence between the position of the axonal and the glial proteins. The results indicate the presence of mechanisms that finely align the cytoskeleton of the axon with the one of the Schwann cells, both at paranodal junctions (with myelin loops) and at nodal gaps (with microvilli). Taken together, our observations reveal the importance of the lateral organization of proteins at the nodes of Ranvier and pave the way for deeper investigations of the molecular ultrastructural mechanisms involved in action potential propagation, the formation of the nodes, axon–glia interactions, and demyelination diseases."],["dc.identifier.doi","10.1073/pnas.1619553114"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13084"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.title","Ultrastructural anatomy of nodes of Ranvier in the peripheral nervous system as revealed by STED microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]