| Literature DB >> 16511095 |
Michael Douglas Lane1, Hyun Joo Nam, Eric Padron, Brittney Gurda-Whitaker, Eric Kohlbrenner, George Aslanidi, Barry Byrne, Robert McKenna, Nicholas Muzyczka, Sergei Zolotukhin, Mavis Agbandje-McKenna.
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.Entities:
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Year: 2005 PMID: 16511095 PMCID: PMC1952340 DOI: 10.1107/S1744309105014132
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091