Structure of human muscle creatine kinase | Zendy

Shen Yuequan | Zendy; Tang Liang | Zendy; Zhou Haimeng | Zendy; Lin Zhengjiong | Zendy

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Structure of human muscle creatine kinase

Author(s) -

Shen Yuequan,

Tang Liang,

Zhou Haimeng,

Lin Zhengjiong

Publication year - 2001

Publication title -

acta crystallographica section d

Language(s) - English

Resource type - Journals

ISSN - 1399-0047

DOI - 10.1107/s0907444901007703

Subject(s) - dimer , creatine kinase , crystal structure , crystallography , monomer , chemistry , creatine , molecular replacement , crystallographic point group , symmetry (geometry) , resolution (logic) , biochemistry , geometry , computer science , mathematics , organic chemistry , polymer , artificial intelligence

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 3 1 axis.

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