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Structure paper

TitleFour decades of structural evolution of GII.4 norovirus
Journal, issue, pagesTo be published
Publish dateMar 24, 2016 (structure data deposition date)
AuthorsSingh, B.K. / Hansman, G.S.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.27 - 2.3 Å
Structure data

PDB-5iyn:
Protruding domain of GII.4 human norovirus CHDC2094
Method: X-RAY DIFFRACTION / Resolution: 1.56 Å

PDB-5iyp:
Protruding domain of GII.4 human norovirus CHDC2094 in complex with HBGA type A (triglycan)
Method: X-RAY DIFFRACTION / Resolution: 1.27 Å

PDB-5iyq:
Protruding domain of GII.4 human norovirus CHDC2094 in complex with HBGA type B (triglycan)
Method: X-RAY DIFFRACTION / Resolution: 1.41 Å

PDB-5kon:
Protruding domain of GII.4 human norovirus isolate 08-14
Method: X-RAY DIFFRACTION / Resolution: 1.51 Å

PDB-5lfe:
Protruding domain of GII.4 human norovirus isolate 8-14 in complex with HBGA type B (triglycan)
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-FLC:
CITRATE ANION

ChemComp-MES:
2-(N-MORPHOLINO)-ETHANESULFONIC ACID / pH buffer*YM

Source
  • norovirus hu/gii.4/chdc2094/1974/us
  • norovirus gii.4
  • norovirus hu/gii.4/sydney/nsw0514/2012/au
KeywordsVIRAL PROTEIN / Norovirus / Virus capsid / Protruding domain / HBGA / Viral capsid protein / Histo-blood group antigen

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