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- W2081279063 abstract "The structure and dimensions of bacteriophage λ have been studied with the freezeetching technique and were compared with those of negatively stained virus. The diameter of the phage head measured 58.0 ± 2.5 nm after negative staining, and 61.5 ± 5.5 nm after freeze-etching. In unfixed preparations, freeze-etching revealed a smooth surface of the head, whereas formaldehyde fixation prior to freeze-etching resulted in well-defined capsomeres. The diameter of the individual capsomeres measured 5.6 ± 0.8 nm, their center-to-center distance 7.4 ± 0.8 nm. Micrographs of λ heads in which two vertices were visible (with each vertex showing one central capsomere surrounded by five neighboring capsomeres), allowed one to study the capsomeric positioning on the capsid and to postulate a triangulation umber (T) of 21, with a right-handed skewness. A model was built accordingly. Our structural data together with biochemical and genetic evidence suggest the presence of several, possibly three, capsid protein units per capsomere. Since there was a surprisingly low incidence (⋍8%) of capsid views in our micrographs revealing simultaneously two vertices, a computer was used to draw capsids in random rotation. These idealized conditions increased the chance for seeing simultaneously two vertices to only about 13%. Stereo views of freezeetched particles as well as of the computer-generated models enhanced this chance slightly, mainly by noise reduction and by the three-dimensional perception of the capsid, thus affirming the relative capsomeric positioning. In a number of freezeetched phage tails helices of opposing handedness were observed, whereas the negatively stained tail revealed the image of “stacked discs.”" @default.
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- W2081279063 date "1973-08-01" @default.
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- W2081279063 title "The capsid structure of bacteriophage lambda" @default.
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- W2081279063 doi "https://doi.org/10.1016/0042-6822(73)90157-8" @default.
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