The major research area of O. Srivastava’s laboratory is the study on the role of cross-links in crystallin protein aggregation during aging and cataractogenesis. Cristallin is the joint name for a family of proteins found in the eye’s crystalline lens and cornea of human and other mammals. Crystallin consists of several individual proteins: αА- and αВ- crystallins are the chaperone proteins maintaining the structure of crystalline lens proteins, and consequently, lens transparency; γ-crystallin is the structural protein found in the lens. The purpose of the study was to determine in vitro cross-linking of gamma D-crystallin fragments alone and with alpha-, beta- and gamma-crystallins. Moreover, the scientists tried to ascertain the existence of covalent multimers of the polypeptide in vivo, and post-translational modifications in the three isoforms of the polypeptide. The study has shown that crystallin fragments are covalently crosslinked via non-disulfide bonding. The polypeptide also exhibited crosslinking with individual alpha-, beta-, and gamma-crystallins. Tryptophan and methionine oxidation are posttranslational modifications of the crystallin polypeptide. So gamma D-crystallin fragment is able to crosslink another fragments and stimulates oxidation of tryptophan and methionine residues. The scientists have found two types of multimers which appear in youth and keep on accumulating during aging. The first type consists of 8 different crystallins (αА, αB etc.). The second type shows the presence of filensin and phakinin proteins in addition to crystallin fragments. Crystallin fragments undergo post-translational modifications. It is found that during cataractogenesis, multimers are accumulating more intensively than in heathy people. Insoluble βA3/A1 and βB1 crystallin fragments were found in the lens of patients with cataract. Further study on different types of crystallin proteins and its modifications found in the crystalline lens is necessary to develop a new treatment for cataract.