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, t he bovine retinal arrestin. Arrestin is essential for the fine regulat ion and termination of the light-induced enzyme cascade in vertebrate rod outer segments. It plays an important role in quenching phototrans duction by its ability to preferentially bind to phosphorylated light- activated rhodopsin. The crystals diffract between 3 Angstrom and 3.5 Angstrom (space group P2(1)2(1)2, cell dimensions a = 169.17 Angstrom, b = 185.53 Angstrom, c = 90.93 Angstrom, T = 100 K). The asymmetric u nit contains four molecules with a solvent content of 68.5% by volume. (C) 1997 Federation of European Biochemical Societies.