Cryogenic optical localization provides 3D protein structure data with Angstrom resolution
Weisenburger S, Boening D, Schomburg B, Giller K, Becker S, Griesinger C, Sandoghdar V (2017)
Publication Type: Journal article
Publication year: 2017
Journal
Book Volume: 14
Pages Range: 141-144
Journal Issue: 2
DOI: 10.1038/nmeth.4141
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.
Authors with CRIS profile
Siegfried Weisenburger
Lehrstuhl für Experimentalphysik
Vahid Sandoghdar
Lehrstuhl für Experimentalphysik
Additional Organisation(s)
Involved external institutions
Max-Planck-Institut für die Physik des Lichts (MPL) / Max Planck Institute for the Science of Light
Germany (DE)
Max-Planck-Institut für biophysikalische Chemie (Karl-Friedrich-Bonhoeffer-Institut) / Max Planck Institute for Biophysical Chemistry
Germany (DE)
Germany (DE)
Max-Planck-Institut für biophysikalische Chemie (Karl-Friedrich-Bonhoeffer-Institut) / Max Planck Institute for Biophysical Chemistry
Germany (DE)
How to cite
APA:
Weisenburger, S., Boening, D., Schomburg, B., Giller, K., Becker, S., Griesinger, C., & Sandoghdar, V. (2017). Cryogenic optical localization provides 3D protein structure data with Angstrom resolution. Nature methods, 14(2), 141-144. https://doi.org/10.1038/nmeth.4141
MLA:
Weisenburger, Siegfried, et al. "Cryogenic optical localization provides 3D protein structure data with Angstrom resolution." Nature methods 14.2 (2017): 141-144.
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