1. Production, purification, crystallization and preliminary X-ray analysis of adeno-associated virus serotype 8
- Author
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Nicholas Muzyczka, Barry J. Byrne, Eric Padron, Robert McKenna, Hyun Joo Nam, George Aslanidi, Michael Douglas Lane, Brittney Gurda-Whitaker, Mavis Agbandje-McKenna, Sergei Zolotukhin, and Eric Kohlbrenner
- Subjects
Insecta ,Viral protein ,viruses ,Biophysics ,Biology ,medicine.disease_cause ,Biochemistry ,law.invention ,Cell Line ,Viral Proteins ,Capsid ,X-Ray Diffraction ,Structural Biology ,law ,Genetics ,medicine ,Animals ,Crystallization ,Cloning, Molecular ,Adeno-associated virus ,Parvovirus ,Resolution (electron density) ,Space group ,Dependovirus ,Condensed Matter Physics ,biology.organism_classification ,Crystallography ,Crystallization Communications ,X-ray crystallography ,Capsid Proteins - 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.
- Published
- 2005