Electron cryomicroscopy methods

Vinzenz M. Unger

doi:10.1016/S0959-440X(00)00260-8

Electron cryomicroscopy methods

Vinzenz M. Unger^*

^*Corresponding author for this work

Molecular Biosciences

Research output: Contribution to journal › Review article › peer-review

37 Scopus citations

Abstract

Electron cryomicroscopy methods comprise a rapidly expanding field providing insights into the structure and function of biological macromolecules and their supramolecular assemblies. The 3.8 Å resolution structure of the membrane protein aquaporin, a view of the herpesvirus capsid at 8.5 Å and the 10 Å resolution structure of the spliceosomal U1 small nuclear ribonucleoprotein complex are three outstanding examples emphasizing the versatility of this technique.

Original language	English (US)
Pages (from-to)	548-554
Number of pages	7
Journal	Current Opinion in Structural Biology
Volume	11
Issue number	5
DOIs	https://doi.org/10.1016/S0959-440X(00)00260-8
State	Published - Sep 1 2001

ASJC Scopus subject areas

Structural Biology
Molecular Biology

Access to Document

10.1016/S0959-440X(00)00260-8

Cite this

@article{e45eebd6a9bc49c49e53064765208cdb,

title = "Electron cryomicroscopy methods",

abstract = "Electron cryomicroscopy methods comprise a rapidly expanding field providing insights into the structure and function of biological macromolecules and their supramolecular assemblies. The 3.8 {\AA} resolution structure of the membrane protein aquaporin, a view of the herpesvirus capsid at 8.5 {\AA} and the 10 {\AA} resolution structure of the spliceosomal U1 small nuclear ribonucleoprotein complex are three outstanding examples emphasizing the versatility of this technique.",

author = "Unger, \{Vinzenz M.\}",

year = "2001",

month = sep,

day = "1",

doi = "10.1016/S0959-440X(00)00260-8",

language = "English (US)",

volume = "11",

pages = "548--554",

journal = "Current Opinion in Structural Biology",

issn = "0959-440X",

publisher = "Elsevier Ltd",

number = "5",

}

TY - JOUR

T1 - Electron cryomicroscopy methods

AU - Unger, Vinzenz M.

PY - 2001/9/1

Y1 - 2001/9/1

N2 - Electron cryomicroscopy methods comprise a rapidly expanding field providing insights into the structure and function of biological macromolecules and their supramolecular assemblies. The 3.8 Å resolution structure of the membrane protein aquaporin, a view of the herpesvirus capsid at 8.5 Å and the 10 Å resolution structure of the spliceosomal U1 small nuclear ribonucleoprotein complex are three outstanding examples emphasizing the versatility of this technique.

AB - Electron cryomicroscopy methods comprise a rapidly expanding field providing insights into the structure and function of biological macromolecules and their supramolecular assemblies. The 3.8 Å resolution structure of the membrane protein aquaporin, a view of the herpesvirus capsid at 8.5 Å and the 10 Å resolution structure of the spliceosomal U1 small nuclear ribonucleoprotein complex are three outstanding examples emphasizing the versatility of this technique.

UR - http://www.scopus.com/inward/record.url?scp=0035442391&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035442391&partnerID=8YFLogxK

U2 - 10.1016/S0959-440X(00)00260-8

DO - 10.1016/S0959-440X(00)00260-8

M3 - Review article

C2 - 11785754

AN - SCOPUS:0035442391

SN - 0959-440X

VL - 11

SP - 548

EP - 554

JO - Current Opinion in Structural Biology

JF - Current Opinion in Structural Biology

IS - 5

ER -

Electron cryomicroscopy methods

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this