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

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.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-DE95-B Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-DE9D-C
Genre: Journal Article

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 Creators:
Weisenburger, S., Author
Boening, D., Author
Schomburg, B.1, Author              
Giller, K.1, Author              
Becker, S.1, Author              
Griesinger, C.1, Author              
Sandoghdar, V., Author
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1Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 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.

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Language(s): eng - English
 Dates: 2017-01-092017-02
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/NMETH.4141
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Title: Nature Methods
Source Genre: Journal
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Pages: - Volume / Issue: 14 (2) Sequence Number: - Start / End Page: 141 - 144 Identifier: -