Production, purification and preliminary X-ray crystallographic studies of adeno-associated virus serotype 7.
Crystals of baculovirus-expressed adeno-associated virus serotype 7 capsids diffract X-rays to approximately 3.0 A resolution. The crystals belong to the rhombohedral space group R3, with unit-cell parameters a = 252.4, c = 591.2 A in the hexagonal setting. The diffraction data were processed and reduced to an overall completeness of 79.0% and an R(merge) of 12.0%. There are three viral capsids in the unit cell. The icosahedral threefold axis is coincident with the crystallographic threefold axis, resulting in one third of a capsid (20 monomers) per crystallographic asymmetric unit. The orientation of the viral capsid has been determined by rotation-function searches and is positioned at (0, 0, 0) by packing considerations.
Quesada
Odayme
O
Department of Biochemistry and Molecular Biology, McKnight Brain Institute, Center for Structural Biology, University of Florida, Gainesville, FL 32610, USA.
Gurda
Brittney
B
Govindasamy
Lakshmanan
L
McKenna
Robert
R
Kohlbrenner
Erik
E
Aslanidi
George
G
Zolotukhin
Sergei
S
Muzyczka
Nicholas
N
Agbandje-McKenna
Mavis
M
D036022:Capsid Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism* / Q000648:ultrastructure; D003460:Crystallization; D000229:Dependovirus / Q000737:chemistry* / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D008854:Microscopy, Electron; D014961:X-Ray Diffraction
D036022:Capsid Proteins