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Electron cryo‐microscopy and image reconstruction of adeno‐associated virus type 2 empty capsids
Author(s) -
Kronenberg Stephanie,
Kleinschmidt Jürgen A,
Böttcher Bettina
Publication year - 2001
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1093/embo-reports/kve234
Subject(s) - capsid , icosahedral symmetry , electron microscope , cryo electron microscopy , parvoviridae , crystallography , resolution (logic) , parvovirus , biophysics , virus , chemistry , microscopy , microbiology and biotechnology , biology , physics , virology , optics , computer science , artificial intelligence
Adeno‐associated virus type 2 empty capsids are composed of three proteins, VP1, VP2 and VP3, which have relative molecular masses of 87, 72 and 62 kDa, respectively, and differ in their N‐terminal amino acid sequences. They have a likely molar ratio of 1:1:8 and occupy symmetrical equivalent positions in an icosahedrally arranged protein shell. We have investigated empty capsids of adeno‐associated virus type 2 by electron cryo‐microscopy and icosahedral image reconstruction. The three‐dimensional map at 1.05 nm resolution showed sets of three elongated spikes surrounding the three‐fold symmetry axes and narrow empty channels at the five‐fold axes. The inside of the capsid superimposed with the previously determined structure of the canine parvovirus ( Q. Xie and M.S. Chapman , 1996 , J. Mol. Biol. , 264 , 497 – 520 ), whereas the outer surface showed clear discrepancies. Globular structures at the inner surface of the capsid at the two‐fold symmetry axes were identified as possible positions for the N‐terminal extensions of VP1 and VP2.