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 approximately 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 A resolution using synchrotron radiation and belong to the hexagonal space group P6(3)22, with unit-cell parameters a = 257.5, c = 443.5 A. The unit cell contains two viral particles, with ten capsid viral protein monomers per crystallographic asymmetric unit.