EMD-33215

Single-particle
4.7 Å
EMD-33215
3D View Gallery
Deposition: 14/04/2022
Map released: 04/05/2022
Last modified: 09/10/2024
Overview 3D View Sample Experiment Validation Additional data Links
Overview 3D View Sample Experiment Validation Additional data Links

EMD-33215

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-7yl9 summary report (pdf.gz) Map-7yl9 FULL report (pdf.gz)

EMDB Annotations

EMICSS entry mapping (xml)

EMDB Files

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

Cryo-EM reconstruction of complete transmembrane channel E289A mutant Vibrio cholerae Cytolysin

EMD-33215

Single-particle
4.7 Å
EMD-33215
3D View Gallery
Deposition: 14/04/2022
Map released: 04/05/2022
Last modified: 09/10/2024
Overview 3D View Sample Experiment Validation Additional data Links
Sample Organism: Vibrio cholerae
Sample: Cryo-EM reconstruction of complete transmembrane channel E289A mutant Vibrio cholerae Cytolysin
Fitted models: 7yl9

Deposition Authors: Mondal AK , Sengupta N, Singh M , Lata K , Lahiri I , Dutta S , Chattopadhyay K
Glu289 residue in the pore-forming motif of Vibrio cholerae cytolysin is important for efficient beta-barrel pore formation.
Mondal AK , Sengupta N, Singh M , Biswas R, Lata K , Lahiri I , Dutta S , Chattopadhyay K
(2022) J Biol Chem , 298 , 102441 - 102441
PUBMED: 36055404
DOI: doi:10.1016/j.jbc.2022.102441
ISSN: 1083-351X
ASTM: JBCHA3