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 abili...

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Bibliographic Details
Published in:FEBS letters 1997-10, Vol.415 (3), p.268-270
Main Authors: Wilden, U., Choe, H.-W., Krafft, B., Granzin, J.
Format: Article
Language:English
Subjects:
Animals
Arrestin
Arrestin - chemistry
Bovine rod outer segment
Cattle
Crystallization
Crystallography, X-Ray
Protein Conformation
Protein Structure, Secondary
Rod Cell Outer Segment - chemistry
X-ray diffraction
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Summary: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 P2 12 12, 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.
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(97)01137-X