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- Title
Crystallization and X-ray diffraction of virus-like particles from a piscine betanodavirus.
- Authors
Luo, Yu-Chun; Wang, Chun-Hsiung; Wu, Yi-Min; Liu, Wangta; Lu, Ming-Wei; Lin, Chan-Shing
- Abstract
Dragon grouper nervous necrosis virus (DGNNV), a member of the genus Betanodavirus, causes high mortality of larvae and juveniles of the grouper fish Epinephelus lanceolatus. Currently, there is no reported crystal structure of a fish nodavirus. The DGNNV virion capsid is derived from a single open reading frame that encodes a 338-amino-acid protein of approximately 37 kDa. The capsid protein of DGNNV was expressed to form virus-like particles (VLPs) in Escherichia coli. The VLP shape is T = 3 quasi-symmetric with a diameter of ∼38 nm in cryo-electron microscopy images and is highly similar to the native virion. In this report, crystals of DGNNV VLPs were grown to a size of 0.27 mm within two weeks by the hanging-drop vapour-diffusion method at 283 K and diffracted X-rays to ∼7.5 Å resolution. In-house X-ray diffraction data of the DGNNV VLP crystals showed that the crystals belonged to space group R32, with unit-cell parameters a = b = 353.00, c = 800.40 Å, α = β = 90, γ = 120°. 23 268 unique reflections were acquired with an overall Rmerge of 18.2% and a completeness of 93.2%. Self-rotation function maps confirmed the fivefold, threefold and twofold symmetries of the icosahedron of DGNNV VLPs.
- Subjects
CRYSTALLIZATION; EPINEPHELUS; FISH larvae; CRYSTAL structure; NODAVIRUSES; X-ray diffraction
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2014, Vol 70, Issue 8, p1080
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X14013703