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- W2061323114 abstract "Adeno-associated viruses (AAVs) are actively being developed for clinical gene-therapy applications and the efficiencies of the vectors could be significantly improved by a detailed understanding of their viral capsid structures and the structural determinants of their tissue-transduction interactions. AAV8 is ∼80% identical to the more widely studied AAV2, but its liver-transduction efficiency is significantly greater than that of AAV2 and other serotypes. The production, purification, crystallization and preliminary X-ray crystallographic analysis of AAV8 viral capsids are reported. The crystals diffract X-rays to 3.0 Å resolution using synchrotron radiation and belong to the hexagonal space group P6322, with unit-cell parameters a = 257.5, c = 443.5 Å. The unit cell contains two viral particles, with ten capsid viral protein monomers per crystallographic asymmetric unit." @default.
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- W2061323114 date "2005-06-01" @default.
- W2061323114 modified "2023-10-14" @default.
- W2061323114 title "Production, purification, crystallization and preliminary X-ray analysis of adeno-associated virus serotype 8" @default.
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- W2061323114 doi "https://doi.org/10.1107/s1744309105014132" @default.
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