Twinned crystals of adeno-associated virus serotype 3b prove suitable for structural studies.
Adeno-associated viruses (AAVs) are leading candidate vectors for gene-therapy applications. The AAV-3b capsid is closely related to the well characterized AAV-2 capsid (87% identity), but sequence and presumably structural differences lead to distinct cell-entry and immune-recognition properties. In an effort to understand these differences and to perhaps harness them, diffraction-quality crystals of purified infectious AAV-3b particles have been grown and several partial diffraction data sets have been recorded. The crystals displayed varying levels of merohedral twinning that in earlier times would have rendered them unsuitable for structure determination, but here is shown to be a tractable complication.
Lerch
Thomas F
TF
Department of Biochemistry and Molecular Biology, School of Medicine, Oregon Health and Science University, Portland, OR 97239-3098, USA.
Xie
Qing
Q
Ongley
Heather M
HM
Hare
Joan
J
Chapman
Michael S
MS
D036022:Capsid Proteins / Q000737:chemistry; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D000229:Dependovirus / Q000737:chemistry* / Q000145:classification* / Q000302:isolation & purification; D006367:HeLa Cells; D006801:Humans; D008956:Models, Chemical; D008958:Models, Molecular; D012703:Serotyping
D036022:Capsid Proteins