Abstract
The protein membranes of the phage T2 head have been isolated in a separate fraction. It has been shown that in an alkaline medium with a pH value of 12.0 to 12.6 the membrane of the phage head dissociates into capsomers with a 5.8 s sedimentation coefficient. Neutralization of the capsomer solution leads to self-assembly of the capsomers with formation of two-dimensional crystal films. The maximum aggregation is observed at pH 4.0, while the increase in ionic strength favours the process of aggregation. By electron microscopy and optical diffraction methods, it has been shown that in the membrane so obtained the subunits are sometimes hexagonally packed with a periodicity of 45 Å.
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