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Updated: Jan 30, 2026

Author Spotlight: High-Throughput Screening to Obtain Crystal Hits for Protein Crystallography
Published on: March 10, 2023
Two-dimensional crystals of carboxysome shell proteins recapitulate the hexagonal packing of three-dimensional
Kelly A Dryden1, Christopher S Crowley, Shiho Tanaka
1Department of Molecular Physiology and Biological Physics, University of Virginia Health System, Charlottesville, Virginia 22908, USA.
Abstract:
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 carboxysome shell proteins assemble spontaneously when His-tagged proteins bind to a monolayer of nickelated lipid molecules at an air-water interface. The molecular packing within the 2D crystals recapitulates the layered hexagonal sheets observed in 3D crystals. The results reinforce current models for the molecular design of BMC shells.
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