@entity1 pathologies often originate from molecular disorders. Therefore, imaging technology as one of the bases for the identification and understanding of pathologies must provide views of single molecules at subnanometer resolution. Membrane proteins mediate many of life's most important processes, and their malfunction is often lethal or leads to severe disease. The membrane proteins @entity21575 ( @entity21575 ) and connexons form junctional microdomains between healthy lens core cells in which @entity21575 form square arrays surrounded by connexons. Malfunction of both proteins results in the formation of @entity231 . We have used high-resolution atomic force microscopy (AFM) to image junctional microdomains in membranes from an individual @entity1 eye lens with senile @entity231 . Images at subnanometer resolution report individual helix-connecting loops of four @entity535 residues on the @entity21575 surface. We describe the supramolecular assembly and the conformational state of @entity21575 in junctional microdomains, where a mixture of truncated junctional and full-length water channel @entity21575 form square arrays. Imaging of microdomain borders revealed individual @entity21575 tetramers and no associated connexon, indicating a lack of metabolite transport, waste accumulation, and enlarged regions of non-adhering membranes, causing @entity231 in this individual. This first high-resolution view of the membrane of this pathological @entity1 tissue provides insights into @entity231 pathology at the single membrane protein level, and indicates the power of the AFM as a future tool in medical imaging at subnanometer resolution.

@entity1 XXXX lens membrane at subnanometer resolution.

@entity1 :: ('9606', 'Species') :: ['human', 'Human'] @entity21575 :: ('4284', 'Gene') :: ['aquaporin-0', 'AQP0'] @entity231 :: ('MESH:D002386', 'Disease') :: ['cataract'] @entity535 :: ('CHEBI:33704', 'Chemical') :: ['amino acid']
@entity231 :: (MESH:D002386,Disease) :: ['cataract']
