EMD-19394

Single-particle
3.52 Å
EMD-19394
3D View Gallery
Deposition: 09/01/2024
Map released: 11/09/2024
Last modified: 11/09/2024
Overview 3D View Sample Experiment Validation Additional data Links
Overview 3D View Sample Experiment Validation Additional data Links

EMD-19394

Archive Files (Depositor)

Primary 3D volume (map.gz) Half-map 1 Half-map 2 (map.gz) Experimental metadata (xml) Experimental metadata (cif.gz)

Validation (wwPDB)

Map-only validation report (pdf.gz) Map-8rnc summary report (pdf.gz) Map-8rnc FULL report (pdf.gz)

EMDB Annotations

EMICSS entry mapping (xml)

EMDB Files

VA raw map (map) VA resolution mask (mrc)

Influenza B polymerase, replication complex, an asymmetric polymerase dimer bound to human ANP32A (from "Influenza B polymerase apo-trimer" | Local refinement)

EMD-19394

Single-particle
3.52 Å
EMD-19394
3D View Gallery
Deposition: 09/01/2024
Map released: 11/09/2024
Last modified: 11/09/2024
Overview 3D View Sample Experiment Validation Additional data Links
Sample Organism: Influenza B virus (B/Memphis/13/2003), Homo sapiens
Sample: Asymmetric dimer of two FluPolB heterotrimers, bridged by human ANP32A
Fitted models: 8rnc

Deposition Authors: Arragain B , Cusack S
Structures of influenza A and B replication complexes give insight into avian to human host adaptation and reveal a role of ANP32 as an electrostatic chaperone for the apo-polymerase.
Arragain B , Krischuns T , Pelosse M , Drncova P, Blackledge M , Naffakh N , Cusack S
(2024) Nat Commun , 15 , 6910 - 6910
PUBMED: 39160148
DOI: doi:10.1038/s41467-024-51007-3
ISSN: 2041-1723