alpha-crystallin, the major protein of the mammalian lens in most species, is an aggregate assembled from two polypeptides, each with a molecular weight around 20,000 Da. It is polydisperse and can be isolated in a variety of forms, including spherical particles with molecular weights ranging upwards from about 200 kDa. Sequence comparisons reveal that it is a member of the small heat shock protein (shsp) family. These proteins are aggregates assembled from polypeptides of 10 to 25 kDa that share a common central domain of about 90 residues (the 'alpha-crystallin domain') with variable N- and C-terminal extensions. alpha-crystallin has been intensively studied for more than 50 years but its three-dimensional structure remains unknown because it has not been possible to obtain crystals for X-ray studies and it is too large for NMR measurements. Structural information has been derived from a variety of solution studies. Because of the protein's polydispersity, interpretation of data has been difficult. This led to different viewpoints and vigorous debate on its structure and properties. Recently, the crystal structures of two closely-related small heat shock proteins have been determined. These have provided some insight into the structure of a-crystallin and explanations of previous observations. Like many other heat shock proteins, alpha-crystallin exhibits chaperone-like properties, including the ability to prevent the precipitation of denatured proteins and to increase cellular tolerance to stress. It has been suggested that these functions are important for the maintenance of lens transparency and the prevention of cataract.