EMD-4809

Single-particle
3.08 Å
EMD-4809 Deposition: 12/04/2019
Map released: 03/07/2019
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Additional data Links
Overview 3D View Sample Experiment Validation Additional data Links

EMD-4809

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-6rd8 summary report (pdf.gz) Map-6rd8 FULL report (pdf.gz)

EMDB Annotations

EMICSS entry mapping (xml)

EMDB Files

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

CryoEM structure of Polytomella F-ATP synthase, c-ring position 2, focussed refinement of Fo and peripheral stalk

EMD-4809

Single-particle
3.08 Å
EMD-4809 Deposition: 12/04/2019
Map released: 03/07/2019
Last modified: 23/10/2024
Overview 3D View Sample Experiment Validation Additional data Links
Sample Organism: Polytomella sp. Pringsheim 198.80
Sample: Polytomella F-ATP synthase subunits ASA1, ASA3, ASA5, ASA6, ASA8, ASA9, ASA10, c-ring and a-subunit.
Fitted models: 6rd8

Deposition Authors: Murphy BJ , Klusch N
Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
Murphy BJ , Klusch N , Langer J , Mills DJ , Yildiz O, Kuhlbrandt W
(2019) Science , 364
PUBMED: 31221832
DOI: doi:10.1126/science.aaw9128
ISSN: 1095-9203
ASTM: SCIEAS