Three-dimensional structure of the hepatitis B core antigen particle truncated at residue 154

Abstract

The three-dimensional structure of recombinant hepatitis B core antigen (HBcAg) particles truncated at residue 154 (HBcAg-154) was determined to 7.8 Å 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. © 2011 Science China Press and Springer-Verlag Berlin Heidelberg.