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Title: Production, Purification, Crystallization and Preliminary X-ray Structural Studies of Adeno-Associated Virus Serotype 5

Abstract

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 Angstroms resolution using synchrotron radiation and belong to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 264.7, b = 447.9, c = 629.7 Angstroms. 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.

Authors:
; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Lab. (BNL), Upton, NY (United States). National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
913918
Report Number(s):
BNL-78486-2007-JA
TRN: US0801403
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Journal Name:
Acta Cryst. F
Additional Journal Information:
Journal Volume: F61
Country of Publication:
United States
Language:
English
Subject:
43 PARTICLE ACCELERATORS; CRYSTALLIZATION; FIBROSIS; GENE THERAPY; ORIENTATION; PRODUCTION; PURIFICATION; RESOLUTION; ROTATION; SPACE GROUPS; SYNCHROTRON RADIATION; national synchrotron light source

Citation Formats

DiMattia, M, Govindasamy, L, Levy, H, Whitaker-Gurda, B, Kohlbrenner, E, Chiorini, J, McKenna, R, Muzyczka, N, Zolotukhin, S, and Agbandje-McKenna, M. Production, Purification, Crystallization and Preliminary X-ray Structural Studies of Adeno-Associated Virus Serotype 5. United States: N. p., 2005. Web. doi:10.1107/S1744309105028514.
DiMattia, M, Govindasamy, L, Levy, H, Whitaker-Gurda, B, Kohlbrenner, E, Chiorini, J, McKenna, R, Muzyczka, N, Zolotukhin, S, & Agbandje-McKenna, M. Production, Purification, Crystallization and Preliminary X-ray Structural Studies of Adeno-Associated Virus Serotype 5. United States. https://doi.org/10.1107/S1744309105028514
DiMattia, M, Govindasamy, L, Levy, H, Whitaker-Gurda, B, Kohlbrenner, E, Chiorini, J, McKenna, R, Muzyczka, N, Zolotukhin, S, and Agbandje-McKenna, M. 2005. "Production, Purification, Crystallization and Preliminary X-ray Structural Studies of Adeno-Associated Virus Serotype 5". United States. https://doi.org/10.1107/S1744309105028514.
@article{osti_913918,
title = {Production, Purification, Crystallization and Preliminary X-ray Structural Studies of Adeno-Associated Virus Serotype 5},
author = {DiMattia, M and Govindasamy, L and Levy, H and Whitaker-Gurda, B and Kohlbrenner, E and Chiorini, J and McKenna, R and Muzyczka, N and Zolotukhin, S and Agbandje-McKenna, M},
abstractNote = {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 Angstroms resolution using synchrotron radiation and belong to the orthorhombic space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 264.7, b = 447.9, c = 629.7 Angstroms. 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.},
doi = {10.1107/S1744309105028514},
url = {https://www.osti.gov/biblio/913918}, journal = {Acta Cryst. F},
number = ,
volume = F61,
place = {United States},
year = {Sat Jan 01 00:00:00 EST 2005},
month = {Sat Jan 01 00:00:00 EST 2005}
}