| abstract |
Protein structures 1 repeating regularly in one, two or three dimensions comprise protein protomers 2 which each comprise at least two monomers 5, 6 genetically fused together. The monomers 5, 6 are monomers of respective oligomer assemblies 3, 4 into which the monomers are assembled to assembly of the protein structure. The first oligomer assembly 3 has rotational symmetry axes including a set of rotational symmetry axes of order N, where N equals 2, 3, 4 or 6. The second oligomer assembly 4 has a rotational symmetry axis of the same order N as said set of rotational symmetry axes of said first oligomer assembly 3 . Due to the symmetry of the oligomer assemblies 3, 4 , the rotational symmetry axis axes of each second oligomer assembly 4 is aligned with one of said set of rotational symmetry axes of a first oligomer assembly 3 with N protomers being arranged symmetrically therearound. Thus, an N-fold fusion between the oligomer assemblies 3, 4 is produced and the arrangements of the rotational symmetry axes of the oligomer assemblies 3, 4 cause the protein structure to repeat regularly. The protein structure has many uses, for example to support molecular entities for x-ray crystallography or electron microscopy. |