EMD-12766

Single-particle
7.8 Å
EMD-12766
3D View Gallery
Deposition: 19/04/2021
Map released: 24/11/2021
Last modified: 10/07/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-12766
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3D volume (map.gz) Experimental metadata (xml) Experimental Metadata (cif.gz)
Map-only Validation report (pdf.gz) Map-only Validation report (cif.gz) Map-only Validation report (xml.gz)
Map and PDB model 7oa6 summary report (pdf.gz) Map and 7oa6 FULL report (pdf.gz)
EMICSS annotations (xml)

Single particle cryo-EM reconstruction of just the top two rings of a 40-mer assembly of recombinant yeast Hsp26 S207E mutant.

EMD-12766

Single-particle
7.8 Å
EMD-12766
3D View Gallery
Deposition: 19/04/2021
Map released: 24/11/2021
Last modified: 10/07/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sample: Top two rings (16 subunits) of a 40mer complex of Hsp26 mutant S207E. (use 0.487 as threshold to visualise)
Fitted models: 7oa6

Deposition Authors: Muehlhofer M, Peters C , Kriehuber T, Kreuzeder M, Kazman P, Rodina N, Reif B , Haslbeck M , Weinkauf S, Buchner J
Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble.
Muhlhofer M, Peters C , Kriehuber T, Kreuzeder M, Kazman P, Rodina N, Reif B , Haslbeck M , Weinkauf S, Buchner J
(2021) Nat Commun , 12 , 6697 - 6697
PUBMED: 34795272
DOI: doi:10.1038/s41467-021-27036-7
ISSN: 2041-1723