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The three-dimensional structure of recombinant hepatitis B core antigen(HBcAg) particles truncated at residue 154(HBcAg-154) was determined to 7.8 ? resolution by cryo-electron microscopy(cryoEM) and computer reconstruction.The capsid of HBcAg-154 is mainly constituted by α-helical folds,highly similar to that of HBcAg-149.The C-terminal region between residues 155 and 183 of the core protein is more crucial to the encapsidation of RNA,and the short C-terminal tail of HBcAg-154 results in a nearly empty capsid.
The three-dimensional structure of recombinant hepatitis B core antigen (HBcAg) particles truncated at residue 154 (HBcAg-154) was determined to 7.8? Resolution by cryo-electron microscopy (cryoEM) and computer reconstruction. Capsid of HBcAg-154 is mainly comprised by α-helical folds, much like to that of HBcAg-149. The C-terminal region between residues 155 and 183 of the core protein is more crucial to the encapsidation of RNA, and the short C-terminal tail of HBcAg-154 results in a nearly empty capsid.