Open AccessProduction, purification, crystallization and preliminary X‐ray structural studies of adeno‐associated virus serotype 5
Author(s) -
DiMattia Michael,
Govindasamy Lakshmanan,
Levy Hazel C.,
GurdaWhitaker Brittney,
Kalina Amy,
Kohlbrenner Erik,
Chiorini John A.,
McKenna Robert,
Muzyczka Nicholas,
Zolotukhin Sergei,
AgbandjeMcKenna Mavis
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309105028514
Subject(s) - adeno associated virus , crystallization , x ray , virology , serotype , materials science , crystallography , biology , chemistry , physics , gene , nuclear physics , recombinant dna , biochemistry , organic chemistry , vector (molecular biology)
Adeno‐associated virus serotype 5 (AAV5) is under development for gene‐therapy applications for the treatment of cystic fibrosis. To elucidate the structural features of AAV5 that control its enhanced transduction of the apical surface of airway epithelia compared with other AAV serotypes, X‐ray crystallographic studies of the viral capsid have been initiated. The production, purification, crystallization and preliminary crystallographic analysis of empty AAV5 viral capsids are reported. The crystals diffract X‐rays to beyond 3.2 Å resolution using synchrotron radiation and belong to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 264.7, b = 447.9, c = 629.7 Å. There is one complete T = 1 viral capsid per asymmetric unit. The orientation and position of the viral capsid in the asymmetric unit have been determined by rotation and translation functions, respectively, and the AAV5 structure determination is in progress.