Loading…

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...

Full description

Saved in:
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:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-c425X-18fbd5b03afab1be7e3ad9732da263a7fba472591bff21ba27e0f3a91cab64983
cites cdi_FETCH-LOGICAL-c425X-18fbd5b03afab1be7e3ad9732da263a7fba472591bff21ba27e0f3a91cab64983
container_end_page 270
container_issue 3
container_start_page 268
container_title FEBS letters
container_volume 415
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
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_79388044</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S001457939701137X</els_id><sourcerecordid>79388044</sourcerecordid><originalsourceid>FETCH-LOGICAL-c425X-18fbd5b03afab1be7e3ad9732da263a7fba472591bff21ba27e0f3a91cab64983</originalsourceid><addsrcrecordid>eNqNkEtr3DAUhUVoSKdpfkJAq9Iu3EiWPbJWpRkyncBAFknBO3FlXwUF25pKninOr4_mQbbtSuicc18fIdecfeeMz28eGeNFVkolvir5jXEuZFafkRmvpMhEMa8-kNl75CP5FOMLS_-KqwtyoURSKzYj9SJMcYSuc68wOj9QGFq6Cdi53g0QJlpnAaakQjdFF6m3FELAOLqB2uB7avzODUiDb6nfjhhoxOceh_EzObfQRbw6vZfk9_LuabHK1g-_7hc_11lT5GWd8cqatjRMgAXDDUoU0Cop8hbyuQBpDRQyLxU31ubcQC6RWQGKN2DmharEJfly7LsJ_s82LaZ7FxvsOhjQb6NOx1cVK4oULI_BJvgYA1q9Ca5PJ2rO9J6oPhDVe1xaSX0gqutUd30asDU9tu9VJ4TJXx39v67D6f-a6uXdbX5w9oaSB3k_6sexFSZgO4dBx8bh0GDrAjajbr37x7JvScycVw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>79388044</pqid></control><display><type>article</type><title>Crystallization and preliminary X-ray analysis of arrestin from bovine rod outer segment</title><source>ScienceDirect Journals</source><source>Wiley-Blackwell Read &amp; Publish Collection</source><creator>Wilden, U. ; Choe, H.-W. ; Krafft, B. ; Granzin, J.</creator><creatorcontrib>Wilden, U. ; Choe, H.-W. ; Krafft, B. ; Granzin, J.</creatorcontrib><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.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(97)01137-X</identifier><identifier>PMID: 9357980</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>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</subject><ispartof>FEBS letters, 1997-10, Vol.415 (3), p.268-270</ispartof><rights>1997 Federation of European Biochemical Societies</rights><rights>FEBS Letters 415 (1997) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c425X-18fbd5b03afab1be7e3ad9732da263a7fba472591bff21ba27e0f3a91cab64983</citedby><cites>FETCH-LOGICAL-c425X-18fbd5b03afab1be7e3ad9732da263a7fba472591bff21ba27e0f3a91cab64983</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S001457939701137X$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3549,27924,27925,45780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9357980$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wilden, U.</creatorcontrib><creatorcontrib>Choe, H.-W.</creatorcontrib><creatorcontrib>Krafft, B.</creatorcontrib><creatorcontrib>Granzin, J.</creatorcontrib><title>Crystallization and preliminary X-ray analysis of arrestin from bovine rod outer segment</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><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.</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 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.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>9357980</pmid><doi>10.1016/S0014-5793(97)01137-X</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 0014-5793
ispartof FEBS letters, 1997-10, Vol.415 (3), p.268-270
issn 0014-5793
1873-3468
language eng
recordid cdi_proquest_miscellaneous_79388044
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
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T10%3A26%3A55IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Crystallization%20and%20preliminary%20X-ray%20analysis%20of%20arrestin%20from%20bovine%20rod%20outer%20segment&rft.jtitle=FEBS%20letters&rft.au=Wilden,%20U.&rft.date=1997-10-06&rft.volume=415&rft.issue=3&rft.spage=268&rft.epage=270&rft.pages=268-270&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/S0014-5793(97)01137-X&rft_dat=%3Cproquest_cross%3E79388044%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c425X-18fbd5b03afab1be7e3ad9732da263a7fba472591bff21ba27e0f3a91cab64983%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=79388044&rft_id=info:pmid/9357980&rfr_iscdi=true