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Expression, purification, crystallization and preliminary X-ray crystallographic studies of hepatitis B virus core fusion protein corresponding to octahedral particles.


ABSTRACT: 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 F432, 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.

SUBMITTER: Kikuchi M 

PROVIDER: S-EPMC3564621 | biostudies-literature | 2013 Feb

REPOSITORIES: biostudies-literature

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Expression, purification, crystallization and preliminary X-ray crystallographic studies of hepatitis B virus core fusion protein corresponding to octahedral particles.

Kikuchi Masaki M   Iwabuchi Shinichiro S   Kikkou Tatsuhiko T   Noguchi Keiichi K   Odaka Masafumi M   Yohda Masafumi M   Kawata Masaaki M   Sato Chikara C   Matsumoto Osamu O  

Acta crystallographica. Section F, Structural biology and crystallization communications 20130131 Pt 2


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 F432, with unit-cell paramet  ...[more]

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