Production, Purification and Preliminary X-ray Crystallographic Studies of Adeno-Associated Virus Serotype 9

Journal Article · Thu Jan 01 04:00:00 EST 2009 · Acta Crystallographica Section F: Structural Biology and Crystallization Communications

DOI:https://doi.org/10.1107/S1744309109021460· OSTI ID:980408

Mitchell, M; Nam, H; Carter, A; McCall, A; Rence, C; Bennett, A; Gurda, B; McKenna, R; Porter, M

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 P32, 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.

• Research Organization: Brookhaven National Laboratory (BNL) National Synchrotron Light Source
• Sponsoring Organization: Doe - Office Of Science
• DOE Contract Number: AC02-98CH10886
• OSTI ID: 980408
• Report Number(s): BNL--93326-2010-JA
• Journal Information: Acta Crystallographica Section F: Structural Biology and Crystallization Communications, Journal Name: Acta Crystallographica Section F: Structural Biology and Crystallization Communications Vol. 65
• Country of Publication: United States
• Language: English

Related Subjects

43 PARTICLE ACCELERATORS
CRYSTALLIZATION
CRYSTALS
EFFICIENCY
MUSCLES
ORIENTATION
PRODUCTION
PURIFICATION
RESOLUTION
SPACE GROUPS
SYNCHROTRON RADIATION
UNITS
USES
national synchrotron light source