Open AccessProduction, purification and preliminary X‐ray crystallographic studies of adeno‐associated virus serotype 9
Author(s) -
Mitchell Matthew,
Nam HyunJoo,
Carter Adam,
McCall Angela,
Rence Chelsea,
Bennett Antonette,
Gurda Brittney,
McKenna Robert,
Porter Mark,
Sakai Yoshihisa,
Byrne Barry J.,
Muzyczka Nicholas,
Aslanidi George,
Zolotukhin Sergei,
AgbandjeMcKenna Mavis
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109021460
Subject(s) - capsid , x ray , transduction (biophysics) , crystallography , molecular replacement , crystallization , synchrotron , resolution (logic) , serotype , virus , adeno associated virus , x ray crystallography , virology , crystal structure , materials science , diffraction , recombinant dna , chemistry , biology , gene , biophysics , physics , optics , genetics , organic chemistry , artificial intelligence , computer science , vector (molecular biology)
Adeno‐associated virus (AAV) serotype 9, which is under development for gene‐delivery applications, shows significantly enhanced capsid‐associated transduction efficiency in muscle compared with other AAV serotypes. With the aim of characterizing the structural determinants of this property, the purification, crystallization and preliminary X‐ray crystallographic analyses of the AAV9 viral capsid are reported. The crystals diffracted X‐rays to 2.8 Å resolution using synchrotron radiation and belonged to the trigonal space group P 3 2 , with unit‐cell parameters a = b = 251.0, c = 640.0 Å. There are three complete viral capsids in the crystal unit cell. The orientation and position of the asymmetric unit capsid have been determined by molecular‐replacement methods and structure determination is in progress.