Schomburg, Benjamin

[["dc.bibliographiccitation.firstpage","141"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Nature Methods"],["dc.bibliographiccitation.lastpage","144"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Weisenburger, Siegfried"],["dc.contributor.author","Boening, Daniel"],["dc.contributor.author","Schomburg, Benjamin"],["dc.contributor.author","Giller, Karin"],["dc.contributor.author","Becker, Stefan"],["dc.contributor.author","Griesinger, Christian"],["dc.contributor.author","Sandoghdar, Vahid"],["dc.date.accessioned","2018-01-17T11:34:28Z"],["dc.date.available","2018-01-17T11:34:28Z"],["dc.date.issued","2017"],["dc.description.abstract","We introduce Cryogenic Optical Localization in 3D (COLD), a method to localize multiple fluorescent sites within a single small protein with Angstrom resolution. We demonstrate COLD by determining the conformational state of the cytosolic Per-ARNT-Sim domain from the histidine kinase CitA of Geobacillus thermodenitrificans and resolving the four biotin sites of streptavidin. COLD provides quantitative 3D information about small- to medium-sized biomolecules on the Angstrom scale and complements other techniques in structural biology."],["dc.identifier.doi","10.1038/nmeth.4141"],["dc.identifier.pii","BFnmeth4141"],["dc.identifier.pmid","28068317"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11681"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.notes.status","final"],["dc.relation.eissn","1548-7105"],["dc.relation.issn","1548-7091"],["dc.rights.uri","http://www.springer.com/tdm"],["dc.title","Cryogenic optical localization provides 3D protein structure data with Angstrom resolution"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]