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Quasi-hexagonal molecular packing in collagen fibrils

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Abstract

Collagen molecules in native 66.8 nm (D) periodic fibrils are widely believed to be assembled into discrete, rope-like sub-structures, or microfibrils1–17. Several types of microfibril have been proposed (2,4,5,7- and 8-stranded), mainly on the basis of information contained in the medium angle X-ray diffraction patterns of native tendon fibres1,5–7. These patterns show a series of equatorial and near-equatorial Bragg reflections which indicate that the collagen molecules are arranged on a three-dimensional crystalline lattice. The 4-stranded11, 5-stranded4–6 and 8-stranded7,8 microfibrils are D-periodic with approximate diameter 3.8 nm, and these and the 2-stranded10 model are supposed to be packed on a three-dimensional lattice whose basal unit cell, (approximately) perpendicular to the fibril axis, is tetragonal (or quasi-tetragonal) with side a, √2 symbol or 2a, where a is ∼ 3.8 nm. In this paper we describe a re-interpretation of the X-ray data5,6 which leads to a new model for the crystalline regions of the fibril, based on quasi-hexagonal molecular packing without microfibrillar sub-structures, and hence having the character of a molecular crystal18.

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Author notes

  1. David J. S. Hulmes

    Present address: EMBL, Grenoble

Authors and Affiliations

  1. European Molecular Biology Laboratory, Grenoble, and Developmental Biology Laboratory, Department of Medicine, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts, 02114

    David J. S. Hulmes

  2. European Molecular Biology Laboratory, Grenoble Outstation, CENG, 85X, 38041, Grenoble Cedex, France

    Andrew Miller

Authors
  1. David J. S. Hulmes
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  2. Andrew Miller
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Hulmes, D., Miller, A. Quasi-hexagonal molecular packing in collagen fibrils. Nature 282, 878–880 (1979). https://doi.org/10.1038/282878a0

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