Danzl, Johann Georg

[["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Gregor, Carola"],["dc.contributor.author","Sidenstein, Sven C."],["dc.contributor.author","Andresen, Martin"],["dc.contributor.author","Sahl, Steffen J."],["dc.contributor.author","Danzl, Johann G."],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2018-04-23T11:48:22Z"],["dc.date.available","2018-04-23T11:48:22Z"],["dc.date.issued","2018"],["dc.description.abstract","The reversibly switchable fluorescent proteins (RSFPs) commonly used for RESOLFT nanoscopy have been developed from fluorescent proteins of the GFP superfamily. These proteins are bright, but exhibit several drawbacks such as relatively large size, oxygen-dependence, sensitivity to low pH, and limited switching speed. Therefore, RSFPs from other origins with improved properties need to be explored. Here, we report the development of two RSFPs based on the LOV domain of the photoreceptor protein YtvA from Bacillus subtilis. LOV domains obtain their fluorescence by association with the abundant cellular cofactor flavin mononucleotide (FMN). Under illumination with blue and ultraviolet light, they undergo a photocycle, making these proteins inherently photoswitchable. Our first improved variant, rsLOV1, can be used for RESOLFT imaging, whereas rsLOV2 proved useful for STED nanoscopy of living cells with a resolution of down to 50 nm. In addition to their smaller size compared to GFP-related proteins (17 kDa instead of 27 kDa) and their usability at low pH, rsLOV1 and rsLOV2 exhibit faster switching kinetics, switching on and off 3 times faster than rsEGFP2, the fastest-switching RSFP reported to date. Therefore, LOV-domain-based RSFPs have potential for applications where the switching speed of GFP-based proteins is limiting."],["dc.identifier.doi","10.1038/s41598-018-19947-1"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13496"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation.issn","2045-2322"],["dc.title","Novel reversibly switchable fluorescent proteins for RESOLFT and STED nanoscopy engineered from the bacterial photoreceptor YtvA"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","122"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Nature Photonics"],["dc.bibliographiccitation.lastpage","128"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Danzl, Johann G."],["dc.contributor.author","Sidenstein, Sven C."],["dc.contributor.author","Gregor, Carola"],["dc.contributor.author","Urban, Nicolai T."],["dc.contributor.author","Ilgen, Peter"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2017-09-07T11:54:41Z"],["dc.date.available","2017-09-07T11:54:41Z"],["dc.date.issued","2016"],["dc.description.abstract","Far-field super-resolution fluorescence microscopy discerns fluorophores residing closer than the diffraction barrier by briefly transferring them in different (typically ON and OFF) states before detection. In coordinate-targeted super-resolution variants, such as stimulated emission depletion (STED) microscopy, this state difference is created by the intensity minima and maxima of an optical pattern, causing all fluorophores to assume the off state, for instance, except at the minima. Although strong spatial confinement of the on state enables high resolution, it also subjects the fluorophores to excess intensities and state cycles at the maxima. Here, we address these issues by driving the fluorophores into a second off state that is inert to the excess light. By using reversibly switchable fluorescent proteins as labels, our approach reduces bleaching and enhances resolution and contrast in live-cell STED microscopy. Using two or more transitions to off states is a useful strategy for augmenting the power of coordinate-targeted super-resolution microscopy."],["dc.identifier.doi","10.1038/NPHOTON.2015.266"],["dc.identifier.gro","3141737"],["dc.identifier.isi","000369321400015"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/513"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: European Union [PIEF-GA-2011-299283]; Korber Foundation"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1749-4893"],["dc.relation.issn","1749-4885"],["dc.title","Coordinate-targeted fluorescence nanoscopy with multiple off states"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","186a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","187a"],["dc.bibliographiccitation.volume","112"],["dc.contributor.author","Danzl, Johann G."],["dc.contributor.author","Sidenstein, Sven"],["dc.contributor.author","Gregor, Carola"],["dc.contributor.author","Urban, Nicolai"],["dc.contributor.author","Ilgen, Peter"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Hell, Stefan"],["dc.date.accessioned","2022-03-01T11:44:58Z"],["dc.date.available","2022-03-01T11:44:58Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1016/j.bpj.2016.11.1034"],["dc.identifier.pii","S0006349516320641"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103178"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0006-3495"],["dc.title","Coordinate-Targeted Fluorescence Nanoscopy with Multiple Off-States"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]