Crystallization and preliminary X-ray diffraction analysis of recombinant hepatitis E virus-like particle.

Molecular and Cellular Biology, University of California, Davis, CA 95616, USA.
Acta Crystallographica Section F Structural Biology and Crystallization Communications (Impact Factor: 0.57). 05/2008; 64(Pt 4):318-22. DOI: 10.1107/S1744309108007197
Source: PubMed

ABSTRACT Hepatitis E virus (HEV) accounts for the majority of enterically transmitted hepatitis infections worldwide. Currently, there is no specific treatment for or vaccine against HEV. The major structural protein is derived from open reading frame (ORF) 2 of the viral genome. A potential oral vaccine is provided by the virus-like particles formed by a protein construct of partial ORF3 protein (residue 70-123) fused to the N-terminus of the ORF2 protein (residues 112-608). Single crystals obtained by the hanging-drop vapour-diffusion method at 293 K diffract X-rays to 8.3 A resolution. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 337, b = 343, c = 346 A, alpha = beta = gamma = 90 degrees , and contain one particle per asymmetric unit.

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