Self-assembly of coherently dynamic, auxetic, two-dimensional protein crystals

Nature. 2016 May 19;533(7603):369-73. doi: 10.1038/nature17633. Epub 2016 May 2.


Two-dimensional (2D) crystalline materials possess unique structural, mechanical and electronic properties that make them highly attractive in many applications. Although there have been advances in preparing 2D materials that consist of one or a few atomic or molecular layers, bottom-up assembly of 2D crystalline materials remains a challenge and an active area of development. More challenging is the design of dynamic 2D lattices that can undergo large-scale motions without loss of crystallinity. Dynamic behaviour in porous three-dimensional (3D) crystalline solids has been exploited for stimuli-responsive functions and adaptive behaviour. As in such 3D materials, integrating flexibility and adaptiveness into crystalline 2D lattices would greatly broaden the functional scope of 2D materials. Here we report the self-assembly of unsupported, 2D protein lattices with precise spatial arrangements and patterns using a readily accessible design strategy. Three single- or double-point mutants of the C4-symmetric protein RhuA were designed to assemble via different modes of intermolecular interactions (single-disulfide, double-disulfide and metal-coordination) into crystalline 2D arrays. Owing to the flexibility of the single-disulfide interactions, the lattices of one of the variants ((C98)RhuA) are essentially defect-free and undergo substantial, but fully correlated, changes in molecular arrangement, yielding coherently dynamic 2D molecular lattices. (C98)RhuA lattices display a Poisson's ratio of -1-the lowest thermodynamically possible value for an isotropic material-making them auxetic.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Aldehyde-Lyases / chemistry*
  • Aldehyde-Lyases / genetics
  • Aldehyde-Lyases / metabolism*
  • Aldehyde-Lyases / ultrastructure
  • Crystallization
  • Disulfides / chemistry
  • Disulfides / metabolism
  • Escherichia coli / chemistry
  • Metals / chemistry
  • Metals / pharmacology
  • Microscopy, Electron, Transmission
  • Models, Molecular
  • Mutant Proteins / chemistry
  • Mutant Proteins / genetics
  • Mutant Proteins / metabolism
  • Mutant Proteins / ultrastructure
  • Pliability* / drug effects
  • Protein Conformation / drug effects
  • Rotation
  • Stress, Mechanical
  • Thermodynamics


  • Disulfides
  • Metals
  • Mutant Proteins
  • Aldehyde-Lyases
  • rhamnulose-1-phosphate adolase