Backbone and side-chain NMR resonance assignments of Ciona intestinalisβ γ-crystallin

The structural [Formula: see text]-crystallin from the tunicate Ciona intestinalis serves as an evolutionary waypoint between ancestral metal cation-binding crystallins and the [Formula: see text] crystallins of the vertebrate eye lens. Ci-[Formula: see text] maintains the metal cation-binding sites of ancestral crystallins while also sharing common structural motifs with vertebrate lens crystallins. Due to its structure and strong interaction with Ca[Formula: see text], Ci-[Formula: see text] is more thermally and chemically stable than vertebrate lens crystallins, making it an ideal starting point for understanding [Formula: see text] crystallins' evolution for molecular stability. In this study, we present the side-chain and updated backbone resonance assignments of Ci-[Formula: see text] with TALOS-N predictions on the H[Formula: see text], H[Formula: see text], C[Formula: see text], C[Formula: see text] and N chemical shifts. These assignments provide a foundation for future studies of metal binding, dynamics, and stability of proteins in the [Formula: see text]-crystallin family.