Amaranth is a crop known for its high quality proteins. 11S Globulin is one of the most abundant and important storage proteins of the amaranth grain. Here, we report the crystal structure of amaranth 11S proglobulin at a final resolution of 2.28 angstrom. It belonged to the space group P6(3) with cell dimensions a = b = 96.6, c = 75.0 angstrom. It contains one asymmetric unit consisting of 372 residues and 100 water molecules. Disordered regions in the model approximately correspond to the variable regions of the 11S globulins. The structure has an extended alpha-helix and beta-barrel domains at both N-terminal and C-terminal regions, which are characteristic of the 11S and 7S globulins. The three dimensional structure suggests that its high thermal stability is due to the cumulative effects of many factors and its good emulsifying property depended on the balance between its surface hydrophobicity and hydrophilicity. (C) 2012 Elsevier Ltd. All rights reserved.