Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension.
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.
Department of Microbiology, Faculty of Biotechnology and Biomolecular Sciences, Universiti Putra Malaysia, 43400 Serdang, Selangor, Malaysia.
Wen Siang
WS
Tan
Iain W
IW
McNae
Kok Lian
KL
Ho
Malcolm D
MD
Walkinshaw
D003460:Crystallization; D018360:Crystallography, X-Ray; D006515:Hepatitis B virus / Q000737:chemistry*; D019590:Nucleocapsid Proteins / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry*; D014771:Virion / Q000737:chemistry*
D019590:Nucleocapsid Proteins; D010446:Peptide Fragments; C099600:nucleocapsid protein, Hepatitis virus