title: Crystallization and preliminary X-ray analysis of arrestin from bovine rod outer segment.
abstract: 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.
authors.affiliation: Forschungszentrum Jülich, Institut für Biologische Informationsverarbeitung, Germany.
authors.forename: U
authors.initials: U
authors.lastname: Wilden
authors.forename: H W
authors.initials: HW
authors.lastname: Choe
authors.forename: B
authors.initials: B
authors.lastname: Krafft
authors.forename: J
authors.initials: J
authors.lastname: Granzin
mesh_terms: D000818:Animals; D019393:Arrestin / Q000737:chemistry*; D002417:Cattle; D003460:Crystallization; D018360:Crystallography, X-Ray; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012374:Rod Cell Outer Segment / Q000737:chemistry*
chemical_list: D019393:Arrestin