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. 1986 Sep;167(3):1025–1034. doi: 10.1128/jb.167.3.1025-1034.1986

Three-dimensional structure of the surface layer protein of Aquaspirillum serpens VHA determined by electron crystallography.

M R Dickson, K H Downing, W H Wu, R M Glaeser
PMCID: PMC215976  PMID: 3745114

Abstract

The three-dimensional structure of the protein which forms the S layer of Aquaspirillum serpens strain VHA has been determined by electron microscopy. Structures have been reconstructed to a resolution of about 1.6 nm for single-layered specimens and about 4 nm for two-layered specimens. The structure, which has hexagonal symmetry, consists of a core in the shape of a cup, with six projections arising from the rim of the cup to join adjacent subunits at the threefold symmetry axes. The model is consistent with edge views of the S layer which have been obtained in this and other work. It is now clear from this work and from three-dimensional reconstructions of other bacterial S layers that a wide diversity exists in the morphology of surface layers.

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Selected References

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