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Cryogenic optical localization provides 3D protein structure data with Angstrom resolution

MPS-Authors
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Weisenburger,  Siegfried
Sandoghdar Division, Max Planck Institute for the Science of Light, Max Planck Society;

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Boening,  Daniel
Sandoghdar Division, Max Planck Institute for the Science of Light, Max Planck Society;

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Schomburg,  Benjamin
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Giller,  Karin
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Becker,  Stefan
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Griesinger,  Christian
Department of NMR Based Structural Biology, MPI for Biophysical Chemistry, Max Planck Society;

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Sandoghdar,  Vahid
Sandoghdar Division, Max Planck Institute for the Science of Light, Max Planck Society;

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Citation

Weisenburger, S., Boening, D., Schomburg, B., Giller, K., Becker, S., Griesinger, C., et al. (2017). Cryogenic optical localization provides 3D protein structure data with Angstrom resolution. NATURE METHODS, 14(2), 141-144. doi:10.1038/NMETH.4141.


Cite as: https://hdl.handle.net/21.11116/0000-0000-8E8B-4
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 thermodenitnficans 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.