volume 67, issue 1, P249-257 1993
DOI: 10.1128/jvi.67.1.249-257.1993
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Abstract: Assembly of hepatitis B virus capsid-like (core) particles occurs efficiently in a variety of heterologous systems via aggregation of-180 molecules of a single 21.5-kDa core protein (p21.5), resulting in an icosahedral capsid structure with T=3 symmetry. Recent studies on the assembly of hepatitis B virus core particles in Xenopus oocytes suggested that dimers of p21.5 represent the major building block from which capsids are generated. Here we determined the concentration dependence of this assembly process. …

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