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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Wilden U,Choe HW,Krafft B,Granzin J

doi

10.1016/s0014-5793(97)01137-x

subject

Has Abstract

pub_date

1997-10-06 00:00:00

pages

268-70

issue

3

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)01137-X

journal_volume

415

pub_type

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