EMD-36182

Single-particle
3.95 Å
EMD-36182
3D View Gallery
Deposition: 15/05/2023
Map released: 28/02/2024
Last modified: 03/04/2024
Overview 3D View Sample Experiment Validation Additional data Links
Overview 3D View Sample Experiment Validation Additional data Links

EMD-36182

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-8je1 summary report (pdf.gz) Map-8je1 FULL report (pdf.gz)

EMDB Annotations

EMICSS entry mapping (xml)

EMDB Files

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

An asymmetry dimer of the Cul2-Rbx1-EloBC-FEM1B ubiquitin ligase complexed with BEX2

EMD-36182

Single-particle
3.95 Å
EMD-36182
3D View Gallery
Deposition: 15/05/2023
Map released: 28/02/2024
Last modified: 03/04/2024
Overview 3D View Sample Experiment Validation Additional data Links
Sample Organism: Homo sapiens
Sample: Neddylated Cul2-Rbx1-EloBC-FEM1B ubiquitin ligase complexed with BEX2
Fitted models: 8je1

Deposition Authors: Dai Z , Liang L , Yin YX
Structural insights into the ubiquitylation strategy of the oligomeric CRL2 FEM1B E3 ubiquitin ligase.
Dai Z , Liang L , Wang W, Zuo P, Yu S , Liu Y , Zhao X, Lu Y , Jin Y, Zhang F, Ding D , Deng W, Yin Y
(2024) EMBO J , 43 , 1089 - 1109
PUBMED: 38360992
DOI: doi:10.1038/s44318-024-00047-y
ISSN: 1460-2075
ASTM: EMJODG