Preliminary X-ray crystallographic analysis of the AAV9 viral capsid showed that the crystals diffracted X-rays to 2.8 A resolution and belonged to the trigonal space group P3(2).
Preliminary X-ray crystallographic analysis of AAV9 provides foundational data for determining its structural determinants, which may inform its use in gene-delivery applications.
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 A resolution using synchrotron radiation and belonged to the trigonal space group P3(2), with unit-cell parameters a = b = 251.0, c = 640.0 A. 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.
Mitchell et al. (2009) studied this question. Adeno-associated virus (AAV) serotype 9 was evaluated on X-ray crystallographic analysis. Preliminary X-ray crystallographic analysis of the AAV9 viral capsid showed that the crystals diffracted X-rays to 2.8 A resolution and belonged to the trigonal space group P3(2).
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