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Adenovirus polypeptide IX revealed as capsid cement by difference images from electron microscopy and crystallography.
Author(s) -
Furcinitti P.S.,
Oostrum J.,
Burnett R.M.
Publication year - 1989
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1989.tb08528.x
Subject(s) - national laboratory , physics , library science , biology , engineering physics , computer science
Particles of adenovirus type 2 (ad2), when disassembled, consistently yield groups‐of‐nine (GON) hexons, which are the major virion shell component. The location of a minor component (6%) of the GON has been determined using a novel combination of electron microscopy and X‐ray crystallography. The Brookhaven Scanning Transmission Electron Microscope (STEM) was used to estimate the distribution of protein in the GON to a resolution of 15‐18 A. The relative hexon positions then were determined to within 1 A using a model of the hexon derived from the X‐ray crystal structure to search the STEM image. The difference image between the STEM image and a model hexon group reveals individual monomers of polypeptide IX extending along the hexon‐‐hexon interfaces. The distribution confirms our earlier proposal that four trimers of polypeptide IX are embedded in the large cavities in the upper surface of the GON to cement hexons into a highly‐stable assembly.