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Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy.


ultrastructure, Escherichia coli, Hepatitis B Core Antigens, Hepatitis B virus, Humans, Cryopreservation, Image Processing, Computer-Assisted, Microscopy, Electron, methods, Protein Conformation, Recombinant Proteins

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      Human hepatitis B virus core protein expressed in E. coli assembles into two sizes of particle. We have determined their three-dimensional structures by electron cryomicroscopy and image processing. The large and small particles correspond to triangulation number T = 4 and T = 3 dimer clustered packings, containing 240 and 180 protein subunits, respectively. The local packing of subunits is very similar in the two sizes of particle and shows holes or channels through the shell. The native viral core particle packages RNA and is active in reverse transcription to DNA. The holes we observe may provide access for the necessary small molecules. Shells assembled from the intact core protein contain additional material, probably RNA, which appears as an icosahedrally ordered inner shell in the three-dimensional map.

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