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

FEBS Letters

Wilden, U.²  Choe, H.-W.¹  Granzin, J.³  Krafft, B.³ 

[1] Department of Chemistry, Natural Science College, Chonbuk National University, 561-756 Chonju, South Korea;Forschungszentrum Jülich, Institut für Biologische Informationsverarbeitung, IBI-1, D-52425 Jülich, Germany;Forschungszentrum Jülich, Institut für Biologische Informationsverarbeitung, IBI-2: Structural Biology, D-52425 Jülich, Germany

关键词: Arrestin;    Bovine rod outer segment;    Crystallization;    X-ray diffraction;   

DOI  :  10.1016/S0014-5793(97)01137-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Å and 3.5 Å (space group P2₁2₁2, cell dimensions a=169.17 Å, b=185.53 Å, c=90.93 Å, T=100 K). The asymmetric unit contains four molecules with a solvent content of 68.5% by volume.

【 授权许可】

Unknown