Two-dimensional crystals of carboxysome shell proteins recapitulate the hexagonal packing of three-dimensional crystals.

@article{Dryden2009TwodimensionalCO,
  title={Two-dimensional crystals of carboxysome shell proteins recapitulate the hexagonal packing of three-dimensional crystals.},
  author={Kelly Dryden and Christopher Sean Crowley and Shiho Tanaka and Todd O. Yeates and Mark Yeager},
  journal={Protein science : a publication of the Protein Society},
  year={2009},
  volume={18 12},
  pages={
          2629-35
        }
}
Bacterial microcompartments (BMCs) are large intracellular bodies that serve as simple organelles in many bacteria. They are proteinaceous structures composed of key enzymes encapsulated by a polyhedral protein shell. In previous studies, the organization of these large shells has been inferred from the conserved packing of the component shell proteins in two-dimensional (2D) layers within the context of three-dimensional (3D) crystals. Here, we show that well-ordered, 2D crystals of… CONTINUE READING
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