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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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Published in: | FEBS letters 1997-10, Vol.415 (3), p.268-270 |
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container_title | FEBS letters |
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creator | Wilden, U. Choe, H.-W. Krafft, B. Granzin, J. |
description | 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. |
doi_str_mv | 10.1016/S0014-5793(97)01137-X |
format | article |
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12
12, cell dimensions
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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.</description><subject>Animals</subject><subject>Arrestin</subject><subject>Arrestin - chemistry</subject><subject>Bovine rod outer segment</subject><subject>Cattle</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Rod Cell Outer Segment - chemistry</subject><subject>X-ray diffraction</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><recordid>eNqNkEtr3DAUhUVoSKdpfkJAq9Iu3EiWPbJWpRkyncBAFknBO3FlXwUF25pKninOr4_mQbbtSuicc18fIdecfeeMz28eGeNFVkolvir5jXEuZFafkRmvpMhEMa8-kNl75CP5FOMLS_-KqwtyoURSKzYj9SJMcYSuc68wOj9QGFq6Cdi53g0QJlpnAaakQjdFF6m3FELAOLqB2uB7avzODUiDb6nfjhhoxOceh_EzObfQRbw6vZfk9_LuabHK1g-_7hc_11lT5GWd8cqatjRMgAXDDUoU0Cop8hbyuQBpDRQyLxU31ubcQC6RWQGKN2DmharEJfly7LsJ_s82LaZ7FxvsOhjQb6NOx1cVK4oULI_BJvgYA1q9Ca5PJ2rO9J6oPhDVe1xaSX0gqutUd30asDU9tu9VJ4TJXx39v67D6f-a6uXdbX5w9oaSB3k_6sexFSZgO4dBx8bh0GDrAjajbr37x7JvScycVw</recordid><startdate>19971006</startdate><enddate>19971006</enddate><creator>Wilden, U.</creator><creator>Choe, H.-W.</creator><creator>Krafft, B.</creator><creator>Granzin, J.</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19971006</creationdate><title>Crystallization and preliminary X-ray analysis of arrestin from bovine rod outer segment</title><author>Wilden, U. ; Choe, H.-W. ; Krafft, B. ; Granzin, J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c425X-18fbd5b03afab1be7e3ad9732da263a7fba472591bff21ba27e0f3a91cab64983</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Arrestin</topic><topic>Arrestin - chemistry</topic><topic>Bovine rod outer segment</topic><topic>Cattle</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Rod Cell Outer Segment - chemistry</topic><topic>X-ray diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wilden, U.</creatorcontrib><creatorcontrib>Choe, H.-W.</creatorcontrib><creatorcontrib>Krafft, B.</creatorcontrib><creatorcontrib>Granzin, J.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wilden, U.</au><au>Choe, H.-W.</au><au>Krafft, B.</au><au>Granzin, J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary X-ray analysis of arrestin from bovine rod outer segment</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1997-10-06</date><risdate>1997</risdate><volume>415</volume><issue>3</issue><spage>268</spage><epage>270</epage><pages>268-270</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><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 Å and 3.5 Å (space group P2
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language | eng |
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source | ScienceDirect Journals; Wiley-Blackwell Read & Publish Collection |
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 |
title | Crystallization and preliminary X-ray analysis of arrestin from bovine rod outer segment |
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