EMD-21383

Single-particle
3.7 Å
EMD-21383
3D View Gallery
Deposition: 13/02/2020
Map released: 08/04/2020
Last modified: 20/11/2024
Overview 3D View Sample Experiment Validation Additional data Links
Overview 3D View Sample Experiment Validation Additional data Links

EMD-21383

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

EMDB Annotations

EMICSS entry mapping (xml)

EMDB Files

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

Cryo-EM Structure of CAP256-VRC26.25 Fab bound to HIV-1 Env trimer CAP256.wk34.c80 SOSIP.RnS2

EMD-21383

Single-particle
3.7 Å
EMD-21383
3D View Gallery
Deposition: 13/02/2020
Map released: 08/04/2020
Last modified: 20/11/2024
Overview 3D View Sample Experiment Validation Additional data Links
Sample Organism: Human immunodeficiency virus 1, Homo sapiens
Sample: Cryo-EM Structure of CAP256-VRC26.25 Fab bound to HIV-1 Env trimer CAP256.wk34.c80 SOSIP.RnS2
Fitted models: 6vtt

Deposition Authors: Gorman J , Kwong PD
Structure of Super-Potent Antibody CAP256-VRC26.25 in Complex with HIV-1 Envelope Reveals a Combined Mode of Trimer-Apex Recognition.
Gorman J , Chuang GY, Lai YT, Shen CH, Boyington JC, Druz A, Geng H, Louder MK, McKee K, Rawi R, Verardi R, Yang Y, Zhang B, Doria-Rose NA, Lin B, Moore PL , Morris L, Shapiro L, Mascola JR, Kwong PD
(2020) Cell Rep , 31 , 107488 - 107488
PUBMED: 32268107
DOI: doi:10.1016/j.celrep.2020.03.052
ISSN: 2211-1247