EMD-5994

Single-particle
13.6 Å
EMD-5994
3D View Gallery
Deposition: 23/06/2014
Map released: 26/11/2014
Last modified: 27/05/2015
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-5994
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3D volume (map.gz) Experimental metadata (xml)
Map-only Validation report (pdf.gz) Map-only Validation report (cif.gz) Map-only Validation report (xml.gz)
Map and PDB model 3j7e summary report (pdf.gz) Map and PDB model 3j7g summary report (pdf.gz) Map and 3j7e FULL report (pdf.gz) Map and 3j7g FULL report (pdf.gz)
EMICSS annotations (xml)

Electron cryo-microscopy of human papillomavirus 16 and H16.V5 Fab fragments

EMD-5994

Single-particle
13.6 Å
EMD-5994
3D View Gallery
Deposition: 23/06/2014
Map released: 26/11/2014
Last modified: 27/05/2015
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Human papillomavirus 16, Mus musculus
Sample: Mature HPV16 quasivirus capsid complexed with H16.V5 Fabs
Fitted models: 3j7e, 3j7g

Deposition Authors: Lee H , Brendle SA, Bywaters SM , Guan J, Ashley RE , Yoder JD, Makhov AM, Conway JF , Christensen ND, Hafenstein S
A CryoEM study identifies the complete H16.V5 epitope and reveals global conformational changes initiated by binding of the neutralizing antibody fragment.
Lee H , Brendle SA, Bywaters SM , Guan J, Ashley RE , Yoder JD, Makhov AM, Conway JF , Christensen ND, Hafenstein S
(2015) J.Virol. , 89 , 1428 - 1438