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. 2018 Jun 5;9:739. doi: 10.3389/fpls.2018.00739

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Copyright © 2018 Fang, Huang, Faulkner, Jiang, Dykes, Yang and Liu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Negative-staining TEM images of isolated recombinant β-carboxysomes. (A) Representative β-carboxysome structures showing the polyhedral shape. The diameter of synthetic β-carboxysomes falls in the range of 200–300 nm. (B) Irregular β-carboxysome structures observed, implying the heterogeneity of recombinant β-carboxysomes. However, the densely packed paracrystalline arrays of interior proteins could be discerned (dash lines). (C) Zoom-in inspection of the paracrystalline arrays depicted in (B, rectangle). (D) Cross-section profile analysis of the paracrystalline arrays illustrates the periodic arrangement of interior proteins. The center-to-center distance between neighboring proteins is ∼10 nm. (E) Fourfold symmetrized correlation average TEM image of the interior protein (top) matches the atomic structure of Rubisco holoenzymes (bottom, PDB: 1UZH), indicating that the observed densely packed interior particles are Rubisco enzymes.