Open AccessExpression, purification, crystallization and preliminary X‐ray crystallographic studies of hepatitis B virus core fusion protein corresponding to octahedral particles
Author(s) -
Kikuchi Masaki,
Iwabuchi Shinichiro,
Kikkou Tatsuhiko,
Noguchi Keiichi,
Odaka Masafumi,
Yohda Masafumi,
Kawata Masaaki,
Sato Chikara,
Matsumoto Osamu
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112052074
Subject(s) - capsid , icosahedral symmetry , crystallization , crystallography , recombinant dna , fusion protein , dimer , octahedron , hepatitis b virus , escherichia coli , protein crystallization , chemistry , materials science , virus , crystal structure , virology , biology , gene , biochemistry , organic chemistry
Recombinant hepatitis B virus core proteins dimerize to form building blocks that are capable of self‐assembly into a capsid. A core capsid protein dimer (CPD) linked to a green fluorescent protein variant, EGFP, at the C‐terminus has been designed. The recombinant fusion CPD was expressed in Escherichia coli , assembled into virus‐like particles (VLPs), purified and crystallized. The single crystal diffracted to 2.15 Å resolution and belonged to the cubic space group F 432, with unit‐cell parameters a = b = c = 219.7 Å. The fusion proteins assembled into icosahedral VLPs in aqueous solution, but were rearranged into octahedral symmetry through the crystal‐packing process under the crystallization conditions.