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Production, purification, crystallization and preliminary X-ray analysis of adeno-associated virus serotype 8

Journal Article · · Acta Crystallographica. Section F
; ; ;  [1]; ;  [2];  [3];  [1];  [3];  [2];  [1]
  1. Department of Biochemistry and Molecular Biology, Center for Structural Biology, McKnight Brain Institute, University of Florida, Gainesville, FL 32610 (United States)
  2. Division of Cell and Molecular Therapy, University of Florida, Gainesville, FL 32610 (United States)
  3. Department of Molecular Genetics and Microbiology and Powell Gene Therapy Center, College of Medicine, University of Florida, Gainesville, FL 32610 (United States)
The production, purification, crystallization and preliminary X-ray crystallographic analysis of adeno-associated virus serotype 8 is reported. 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 P6{sub 3}22, 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.
OSTI ID:
22356034
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 6 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English

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