6E9D
Sub-2 Angstrom Ewald Curvature-Corrected Single-Particle Cryo-EM Reconstruction of AAV-2 L336C
This is a non-PDB format compatible entry.
Summary for 6E9D
Entry DOI | 10.2210/pdb6e9d/pdb |
EMDB information | 9012 |
Descriptor | Capsid protein VP1 (2 entities in total) |
Functional Keywords | aav-2 l336c, gene therapy, ewald sphere curvature correction, per particle ctf, virus like particle |
Biological source | Adeno-associated virus 2 Srivastava/1982 (AAV-2) |
Total number of polymer chains | 60 |
Total formula weight | 4921280.16 |
Authors | Tan, Y.Z.,Aiyer, S.,Mietzsch, M.,Hull, J.A.,McKenna, R.,Baker, T.S.,Agbandje-McKenna, M.,Lyumkis, D. (deposition date: 2018-07-31, release date: 2018-08-15, Last modification date: 2024-03-13) |
Primary citation | Tan, Y.Z.,Aiyer, S.,Mietzsch, M.,Hull, J.A.,McKenna, R.,Grieger, J.,Samulski, R.J.,Baker, T.S.,Agbandje-McKenna, M.,Lyumkis, D. Sub-2 angstrom Ewald curvature corrected structure of an AAV2 capsid variant. Nat Commun, 9:3628-3628, 2018 Cited by PubMed Abstract: Single-particle cryogenic electron microscopy (cryo-EM) provides a powerful methodology for structural biologists, but the resolutions typically attained with experimentally determined structures have lagged behind microscope capabilities. Here, we exploit several technical advances to improve resolution, including per-particle contrast transfer function (CTF) refinement and correction for Ewald sphere curvature. The latter is demonstrated with several experimental samples and should become more standard as resolutions increase or at lower microscope accelerating voltages. The combined application of the described methods to micrographs recorded on a Titan Krios enables structure determination at ~1.86-Å resolution of an adeno-associated virus serotype 2 variant (AAV2), an important gene-delivery vehicle. The resulting structural details provide an improved model for understanding the biology of AAV that will guide future vector development for gene therapy. PubMed: 30194371DOI: 10.1038/s41467-018-06076-6 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (1.86 Å) |
Structure validation
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