short communications
The crystal structure of human muscle creatine kinase has been determined by the molecular-replacement method and refined at 3.5 Å resolution. The structures of both the monomer and the dimer closely resemble those of the other known structures in the creatine kinase family. Two types of dimers, one with a non-crystallographic twofold symmetry axis and the other with a crystallographic twofold symmetry axis, were found to occur simultaneously in the crystal. These dimers form an infinite `double-helix'-like structure along an unusual long crystallographic 31 axis.
Keywords: human muscle creatine kinase.
Supporting information
Portable Document Format (PDF) file https://doi.org/10.1107/S0907444901007703/gr2148sup1.pdf |
PDB reference: human muscle creatine kinase, 1i0e