Beyond structures of highly symmetric purified viral capsids by cryo-EM

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Stass , R , Ilca , S L & Huiskonen , J T 2018 , ' Beyond structures of highly symmetric purified viral capsids by cryo-EM ' , Current Opinion in Structural Biology , vol. 52 , pp. 25-31 . https://doi.org/10.1016/j.sbi.2018.07.011

Title: Beyond structures of highly symmetric purified viral capsids by cryo-EM
Author: Stass, Robert; Ilca, Serban L.; Huiskonen, Juha T.
Contributor: University of Helsinki, Helsinki Institute of Life Science HiLIFE
Date: 2018-10
Language: eng
Number of pages: 7
Belongs to series: Current Opinion in Structural Biology
ISSN: 0959-440X
URI: http://hdl.handle.net/10138/304292
Abstract: Cryogenic transmission electron microscopy (cryo-EM) is widely used to determine high-resolution structures of symmetric virus capsids. The method holds promise for extending studies beyond purified capsids and their symmetric protein shells, The non-symmetric genome component has been addressed in dsRNA cypoviruses and ssRNA bacteriophages Q beta and MS2. The structure of human herpes simplex virus type 1 capsids has been determined within intact virions to resolve capsid-tegument interactions. Electron tomography under cryogenic conditions (cryo-ET), has allowed resolving an early membrane fusion intermediate of Rift Valley fever virus. Antibody-affinity based sample grids allow capturing of virions directly from cell cultures or even clinical samples. These and other emerging methods will support studies to address viral entry, assembly and neutralization processes at increasingly high resolutions and native conditions.
Subject: IN-SITU STRUCTURES
VIRUS
PROTEIN
GENOME
REVEALS
1182 Biochemistry, cell and molecular biology
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