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Production, purification and preliminary X-ray crystallographic studies of adeno-associated virus serotype 7.


ABSTRACT: 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.

SUBMITTER: Quesada O 

PROVIDER: S-EPMC2344100 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature

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Production, purification and preliminary X-ray crystallographic studies of adeno-associated virus serotype 7.

Quesada Odayme O   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  

Acta crystallographica. Section F, Structural biology and crystallization communications 20071130 Pt 12


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 axi  ...[more]

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