Structural studies of virus-antibody complexes by electron cryomicroscopy and X-ray crystallography

Wah Chiu; Thomas J. Smith

doi:10.1016/S0959-440X(94)90311-5

Structural studies of virus-antibody complexes by electron cryomicroscopy and X-ray crystallography

Wah Chiu, Thomas J. Smith

Research output: Contribution to journal › Article › peer-review

9 Scopus citations

Abstract

The combined use of electron cryomicroscopy and X-ray crystallography has recently provided unprecedented and unique structural information of virus-antibody complexes. Different kinds of viral proteins have been located and identified on the capsid surface, certain residues of the viral proteins involved in antibody interactions have been identified; the elbow angle of bound antibody has been measured; and the mechanism of antibody-mediated neutralization has been elucidated. Within the next few years, this combined methodology should help investigators resolve the structures of large macromolecular assemblies to even higher resolutions.

Original language	English (US)
Pages (from-to)	219-224
Number of pages	6
Journal	Current Opinion in Structural Biology
Volume	4
Issue number	2
DOIs	https://doi.org/10.1016/S0959-440X(94)90311-5
State	Published - 1994
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/S0959-440X(94)90311-5

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title = "Structural studies of virus-antibody complexes by electron cryomicroscopy and X-ray crystallography",

abstract = "The combined use of electron cryomicroscopy and X-ray crystallography has recently provided unprecedented and unique structural information of virus-antibody complexes. Different kinds of viral proteins have been located and identified on the capsid surface, certain residues of the viral proteins involved in antibody interactions have been identified; the elbow angle of bound antibody has been measured; and the mechanism of antibody-mediated neutralization has been elucidated. Within the next few years, this combined methodology should help investigators resolve the structures of large macromolecular assemblies to even higher resolutions.",

author = "Wah Chiu and Smith, {Thomas J.}",

note = "Funding Information: We thank the WM Keck Foundation, the National Science Foundation (BR9202199), the National Center for Research Resources (RR02250), and the National Institute of General Medical Sciences (GM10704) for financial support. We also thank Pamela Paradis Powell for her editorial review.",

year = "1994",

doi = "10.1016/S0959-440X(94)90311-5",

language = "English (US)",

volume = "4",

pages = "219--224",

journal = "Current Opinion in Structural Biology",

issn = "0959-440X",

publisher = "Elsevier Ltd",

number = "2",

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T1 - Structural studies of virus-antibody complexes by electron cryomicroscopy and X-ray crystallography

AU - Chiu, Wah

AU - Smith, Thomas J.

N1 - Funding Information: We thank the WM Keck Foundation, the National Science Foundation (BR9202199), the National Center for Research Resources (RR02250), and the National Institute of General Medical Sciences (GM10704) for financial support. We also thank Pamela Paradis Powell for her editorial review.

PY - 1994

Y1 - 1994

N2 - The combined use of electron cryomicroscopy and X-ray crystallography has recently provided unprecedented and unique structural information of virus-antibody complexes. Different kinds of viral proteins have been located and identified on the capsid surface, certain residues of the viral proteins involved in antibody interactions have been identified; the elbow angle of bound antibody has been measured; and the mechanism of antibody-mediated neutralization has been elucidated. Within the next few years, this combined methodology should help investigators resolve the structures of large macromolecular assemblies to even higher resolutions.

AB - The combined use of electron cryomicroscopy and X-ray crystallography has recently provided unprecedented and unique structural information of virus-antibody complexes. Different kinds of viral proteins have been located and identified on the capsid surface, certain residues of the viral proteins involved in antibody interactions have been identified; the elbow angle of bound antibody has been measured; and the mechanism of antibody-mediated neutralization has been elucidated. Within the next few years, this combined methodology should help investigators resolve the structures of large macromolecular assemblies to even higher resolutions.

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JO - Current Opinion in Structural Biology

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IS - 2

ER -

Structural studies of virus-antibody complexes by electron cryomicroscopy and X-ray crystallography

Abstract

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