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Seeing the Herpesvirus Capsid at 8.5 Å

Zhou, Z. Hong, Dougherty, Matthew, Jakana, Joanita, He, Jing, Rixon, Frazer J., Chiu, Wah·2000·Science

Abstract

Human herpesviruses are large and structurally complex viruses that cause a variety of diseases. The three-dimensional structure of the herpesvirus capsid has been determined at 8.5 angstrom resolution by electron cryomicroscopy. More than 30 putative α helices were identified in the four proteins that make up the 0.2 billion–dalton shell. Some of these helices are located at domains that undergo conformational changes during capsid assembly and DNA packaging. The unique spatial arrangement of the heterotrimer at the local threefold positions accounts for the asymmetric interactions with adjacent capsid components and the unusual co-dependent folding of its subunits.

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Metadata

Authors
Zhou, Z. H., Dougherty, M., Jakana, J., He, J., Rixon, F. J., & Chiu, W.
Venue
Science
Published
2000-05-05
Volume
288
Issue
5467
Pages
877-880
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2149476505
Cited by
317
References
0
FWCI
21.29
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Seeing the Herpesvirus Capsid at 8.5 Å. https://app.cochat.ai/papers/10.1126/science.288.5467.877
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Zhou, Z. H., Dougherty, M., Jakana, J., He, J., Rixon, F. J., & Chiu, W. (2000). Seeing the Herpesvirus Capsid at 8.5 Å. Science. https://doi.org/10.1126/science.288.5467.877

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.