TY - JOUR
T1 - Production, purification, crystallization and preliminary X-ray analysis of adeno-associated virus serotype 8
AU - Lane, Michael Douglas
AU - Nam, Hyun Joo
AU - Padron, Eric
AU - Gurda-Whitaker, Brittney
AU - Kohlbrenner, Eric
AU - Aslanidi, George
AU - Byrne, Barry
AU - McKenna, Robert
AU - Muzyczka, Nicholas
AU - Zolotukhin, Sergei
AU - Agbandje-McKenna, Mavis
PY - 2005
Y1 - 2005
N2 - 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.
AB - 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.
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U2 - 10.1107/S1744309105014132
DO - 10.1107/S1744309105014132
M3 - Article
C2 - 16511095
AN - SCOPUS:33744474585
SN - 1744-3091
VL - 61
SP - 558
EP - 561
JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications
IS - 6
ER -