Background: Abnormal glycosylation of a-dystroglycan causes many diseases, such as congenital muscular dystrophies. Determining the a-dystroglycan structure is very important for elucidating the pathogenesis of these disorders and treating them.

Methods: In this study, a-dystroglycan was purified using DEAE (diethylaminoethyl) Sephacel anion-exchange chromatography, WGA (Wheat Germ Agglutinin) affinity chromatography, and size-exclusion chromatography.

Results: The three-dimensional structure of a-dystroglycan was studied using negative staining and single-particle analysis, which revealed two globular domains connected by a flexible linker. The three-dimensional structure of a-dystroglycan is consistent with previously reported 2D images.

Conclusion: Clarifying the three-dimensional structure presented here of a-dystroglycan will help to reveal the molecular mechanisms underlying a-dystroglycanopathy and facilitate its treatment.