Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt 8):642-7. doi: 10.1107/S1744309107033726. Epub 2007 Jul 21.

Abstract

Hepatitis B core (HBc) particles have been extensively exploited as carriers for foreign immunological epitopes in the development of multicomponent vaccines and diagnostic reagents. Crystals of the T = 4 HBc particle were grown in PEG 20,000, ammonium sulfate and various types of alcohols. A temperature jump from 277 or 283 to 290 K was found to enhance crystal growth. A crystal grown using MPD as a cryoprotectant diffracted X-rays to 7.7 A resolution and data were collected to 99.6% completeness at 8.9 A. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 352.3, b = 465.5, c = 645.0 A. The electron-density map reveals a protrusion that is consistent with the N-terminus extending out from the surface of the capsid. The structure presented here supports the idea that N-terminal insertions can be exploited in the development of diagnostic reagents, multicomponent vaccines and delivery vehicles into mammalian cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Hepatitis B virus / chemistry*
  • Nucleocapsid Proteins / chemistry*
  • Peptide Fragments / chemistry*
  • Virion / chemistry*

Substances

  • Nucleocapsid Proteins
  • Peptide Fragments
  • nucleocapsid protein, Hepatitis virus

Associated data

  • PDB/2QIJ