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

Wen Siang Tan, Iain W McNae, Kok Lian Ho, Malcolm D Walkinshaw

Research output: Contribution to journalArticlepeer-review

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.
Original languageEnglish
Article numberF63
Pages (from-to)642-647
Number of pages6
JournalActa Crystallographica Section F Structural Biology and Crystallization Communications
Volume63
Issue numberPt 8
DOIs
Publication statusPublished - 2007

Keywords

  • hepatitis B core particles
  • cryoprotectant
  • temperature jump
  • N-terminal fusion

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