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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 DOI10.2210/pdb6e9d/pdb
EMDB information9012
DescriptorCapsid protein VP1 (2 entities in total)
Functional Keywordsaav-2 l336c, gene therapy, ewald sphere curvature correction, per particle ctf, virus like particle
Biological sourceAdeno-associated virus 2 Srivastava/1982 (AAV-2)
Total number of polymer chains60
Total formula weight4921280.16
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 citationTan, 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: 30194371
DOI: 10.1038/s41467-018-06076-6
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (1.86 Å)
Structure validation

237735

数据于2025-06-18公开中

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