The aggregation of crystallin proteins in the human lens is the primary cause of cataracts, however, the molecular architectures of these structures have not been well understood. Here, the authors use cryo-EM to reveal the near-atomic structure of thin fibrils of human αA-crystallin harboring the pathological R116C mutation formed in vitro under acidic conditions, showing a three-layered structure stabilized by extensive steric zipper interactions.
- Meinai Song
- Jianting Han
- Qin Cao
