| Literature DB >> 19574648 |
Matthew Mitchell1, Hyun-Joo Nam, Adam Carter, Angela McCall, Chelsea Rence, Antonette Bennett, Brittney Gurda, Robert McKenna, Mark Porter, Yoshihisa Sakai, Barry J Byrne, Nicholas Muzyczka, George Aslanidi, Sergei Zolotukhin, Mavis Agbandje-McKenna.
Abstract
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.Entities:
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Year: 2009 PMID: 19574648 PMCID: PMC2705643 DOI: 10.1107/S1744309109021460
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091