Crystallization and preliminary X-ray analysis of arrestin from bovine rod outer segment.

We present the first X-ray study of a member of the arrestin family, the bovine retinal arrestin. Arrestin is essential for the fine regulation and termination of the light-induced enzyme cascade in vertebrate rod outer segments. It plays an important role in quenching phototransduction by its ability to preferentially bind to phosphorylated light-activated rhodopsin. The crystals diffract between 3 angstroms and 3.5 angstroms (space group P2(1)2(1)2, cell dimensions a = 169.17 angstroms, b = 185.53 angstroms, c = 90.93 angstroms, T = 100 K). The asymmetric unit contains four molecules with a solvent content of 68.5% by volume.