Purification, crystallization and preliminary crystallographic studies of a calmodulin-OLFp hybrid molecule
A hybrid molecule consisting of calmodulin (CaM) and the CaM‐binding domain of olfactory nucleotide‐gated ion‐channel peptide (CaM‐OLFp) was purified and crystallized by the hanging‐drop vapour‐diffusion method at 298 K. The crystals diffracted to a maximum resolution of 1.85 Å at cryogenic temperat...
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Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-08, Vol.61 (8), p.785-787 |
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container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
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creator | Chyan, Chia-Lin Huang, Po-Chung Lin, Ta-Hsien Huang, Jian-Wen Lin, S. S. Huang, Hsien-bin Chen, Yi-Cheng |
description | A hybrid molecule consisting of calmodulin (CaM) and the CaM‐binding domain of olfactory nucleotide‐gated ion‐channel peptide (CaM‐OLFp) was purified and crystallized by the hanging‐drop vapour‐diffusion method at 298 K. The crystals diffracted to a maximum resolution of 1.85 Å at cryogenic temperature (100 K) using X‐rays from a rotating anode (Cu, wavelength 1.54 Å). The crystal belongs to the monoclinic space group C2, with unit‐cell parameters a = 64.76, b = 36.23, c = 70.96 Å, α = γ = 90, β = 109.4°. Analysis of the packing density shows that the asymmetric unit contains one CaM‐OLFp hybrid molecule with a solvent content of 36.42%. |
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S. ; Huang, Hsien-bin ; Chen, Yi-Cheng</creator><creatorcontrib>Chyan, Chia-Lin ; Huang, Po-Chung ; Lin, Ta-Hsien ; Huang, Jian-Wen ; Lin, S. S. ; Huang, Hsien-bin ; Chen, Yi-Cheng</creatorcontrib><description>A hybrid molecule consisting of calmodulin (CaM) and the CaM‐binding domain of olfactory nucleotide‐gated ion‐channel peptide (CaM‐OLFp) was purified and crystallized by the hanging‐drop vapour‐diffusion method at 298 K. The crystals diffracted to a maximum resolution of 1.85 Å at cryogenic temperature (100 K) using X‐rays from a rotating anode (Cu, wavelength 1.54 Å). The crystal belongs to the monoclinic space group C2, with unit‐cell parameters a = 64.76, b = 36.23, c = 70.96 Å, α = γ = 90, β = 109.4°. Analysis of the packing density shows that the asymmetric unit contains one CaM‐OLFp hybrid molecule with a solvent content of 36.42%.</description><identifier>ISSN: 1744-3091</identifier><identifier>EISSN: 1744-3091</identifier><identifier>DOI: 10.1107/S1744309105023006</identifier><identifier>PMID: 16511158</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers</publisher><subject>Animals ; ANODES ; Calmodulin - chemistry ; calmodulin-binding domains ; calmodulin-OLFp hybrid molecule ; Chickens ; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY ; CRYSTALLIZATION ; Crystallization Communications ; Crystallography, X-Ray ; CRYSTALS ; Cyclic Nucleotide-Gated Cation Channels ; DENSITY ; DIFFUSION ; HYBRIDIZATION ; Ion Channels - chemistry ; IONS ; MOLECULES ; Recombinant Fusion Proteins - chemistry ; RESOLUTION ; SOLVENTS ; SPACE GROUPS ; STOWING ; WAVELENGTHS</subject><ispartof>Acta crystallographica. Section F, Structural biology and crystallization communications, 2005-08, Vol.61 (8), p.785-787</ispartof><rights>International Union of Crystallography 2005 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5139-a96b4755c97c299decf72b82791f1f4a2920ce171bf3078f28068e10818cb963</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1952352/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1952352/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,27901,27902,45550,45551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16511158$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/22356046$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Chyan, Chia-Lin</creatorcontrib><creatorcontrib>Huang, Po-Chung</creatorcontrib><creatorcontrib>Lin, Ta-Hsien</creatorcontrib><creatorcontrib>Huang, Jian-Wen</creatorcontrib><creatorcontrib>Lin, S. S.</creatorcontrib><creatorcontrib>Huang, Hsien-bin</creatorcontrib><creatorcontrib>Chen, Yi-Cheng</creatorcontrib><title>Purification, crystallization and preliminary crystallographic studies of a calmodulin-OLFp hybrid molecule</title><title>Acta crystallographica. Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><description>A hybrid molecule consisting of calmodulin (CaM) and the CaM‐binding domain of olfactory nucleotide‐gated ion‐channel peptide (CaM‐OLFp) was purified and crystallized by the hanging‐drop vapour‐diffusion method at 298 K. The crystals diffracted to a maximum resolution of 1.85 Å at cryogenic temperature (100 K) using X‐rays from a rotating anode (Cu, wavelength 1.54 Å). The crystal belongs to the monoclinic space group C2, with unit‐cell parameters a = 64.76, b = 36.23, c = 70.96 Å, α = γ = 90, β = 109.4°. Analysis of the packing density shows that the asymmetric unit contains one CaM‐OLFp hybrid molecule with a solvent content of 36.42%.</description><subject>Animals</subject><subject>ANODES</subject><subject>Calmodulin - chemistry</subject><subject>calmodulin-binding domains</subject><subject>calmodulin-OLFp hybrid molecule</subject><subject>Chickens</subject><subject>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</subject><subject>CRYSTALLIZATION</subject><subject>Crystallization Communications</subject><subject>Crystallography, X-Ray</subject><subject>CRYSTALS</subject><subject>Cyclic Nucleotide-Gated Cation Channels</subject><subject>DENSITY</subject><subject>DIFFUSION</subject><subject>HYBRIDIZATION</subject><subject>Ion Channels - chemistry</subject><subject>IONS</subject><subject>MOLECULES</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>RESOLUTION</subject><subject>SOLVENTS</subject><subject>SPACE GROUPS</subject><subject>STOWING</subject><subject>WAVELENGTHS</subject><issn>1744-3091</issn><issn>1744-3091</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUcFu1DAQtRCIloUP4IIiIfVEwGPHcXxBqiq2BRZaiQKCi-U4dtfUiYOdAMvXkyWrpYgD0kgevXnvjUcPoYeAnwJg_uwd8KKgWABmmFCMy1vocAvlW-z2jf4A3UvpC8aUirK6iw6gZADAqkN0fTFGZ51Wgwvdk0zHTRqU9-7nbyBTXZP10XjXuk7FzX4erqLq105naRgbZ1IWbKYyrXwbmtG7Lj9fLftsvamja7I2eKNHb-6jO1b5ZB7s3gW6XL64PDnLV-enL0-OV7lmQEWuRFkXnDEtuCZCNEZbTuqKcAEWbKGIIFgb4FBbinllSYXLygCuoNK1KOkCPZ9t-7FuTaNNN0TlZR9dO50gg3Ly70nn1vIqfJMgGKFTLdDj2SCkwcmk3WD0WoeuM3qQZKKUuNiuOdqtieHraNIgW5e08V51JoxJcgyUQQETEWaijiGlaOz-K4DlNkf5T46T5tHNG_4odsFNBDETvjtvNv93lMefluTiPcOVmLT5rHVpMD_2WhWvZckpZ_Lj21O5_Mw_nNE3r-Ur-gvYCLm3</recordid><startdate>200508</startdate><enddate>200508</enddate><creator>Chyan, Chia-Lin</creator><creator>Huang, Po-Chung</creator><creator>Lin, Ta-Hsien</creator><creator>Huang, Jian-Wen</creator><creator>Lin, S. S.</creator><creator>Huang, Hsien-bin</creator><creator>Chen, Yi-Cheng</creator><general>Munksgaard International Publishers</general><general>International Union of Crystallography</general><scope>BSCLL</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><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>200508</creationdate><title>Purification, crystallization and preliminary crystallographic studies of a calmodulin-OLFp hybrid molecule</title><author>Chyan, Chia-Lin ; Huang, Po-Chung ; Lin, Ta-Hsien ; Huang, Jian-Wen ; Lin, S. S. ; Huang, Hsien-bin ; Chen, Yi-Cheng</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5139-a96b4755c97c299decf72b82791f1f4a2920ce171bf3078f28068e10818cb963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animals</topic><topic>ANODES</topic><topic>Calmodulin - chemistry</topic><topic>calmodulin-binding domains</topic><topic>calmodulin-OLFp hybrid molecule</topic><topic>Chickens</topic><topic>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</topic><topic>CRYSTALLIZATION</topic><topic>Crystallization Communications</topic><topic>Crystallography, X-Ray</topic><topic>CRYSTALS</topic><topic>Cyclic Nucleotide-Gated Cation Channels</topic><topic>DENSITY</topic><topic>DIFFUSION</topic><topic>HYBRIDIZATION</topic><topic>Ion Channels - chemistry</topic><topic>IONS</topic><topic>MOLECULES</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>RESOLUTION</topic><topic>SOLVENTS</topic><topic>SPACE GROUPS</topic><topic>STOWING</topic><topic>WAVELENGTHS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chyan, Chia-Lin</creatorcontrib><creatorcontrib>Huang, Po-Chung</creatorcontrib><creatorcontrib>Lin, Ta-Hsien</creatorcontrib><creatorcontrib>Huang, Jian-Wen</creatorcontrib><creatorcontrib>Lin, S. S.</creatorcontrib><creatorcontrib>Huang, Hsien-bin</creatorcontrib><creatorcontrib>Chen, Yi-Cheng</creatorcontrib><collection>Istex</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><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Chyan, Chia-Lin</au><au>Huang, Po-Chung</au><au>Lin, Ta-Hsien</au><au>Huang, Jian-Wen</au><au>Lin, S. S.</au><au>Huang, Hsien-bin</au><au>Chen, Yi-Cheng</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification, crystallization and preliminary crystallographic studies of a calmodulin-OLFp hybrid molecule</atitle><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle><addtitle>Acta Cryst. F</addtitle><date>2005-08</date><risdate>2005</risdate><volume>61</volume><issue>8</issue><spage>785</spage><epage>787</epage><pages>785-787</pages><issn>1744-3091</issn><eissn>1744-3091</eissn><abstract>A hybrid molecule consisting of calmodulin (CaM) and the CaM‐binding domain of olfactory nucleotide‐gated ion‐channel peptide (CaM‐OLFp) was purified and crystallized by the hanging‐drop vapour‐diffusion method at 298 K. The crystals diffracted to a maximum resolution of 1.85 Å at cryogenic temperature (100 K) using X‐rays from a rotating anode (Cu, wavelength 1.54 Å). The crystal belongs to the monoclinic space group C2, with unit‐cell parameters a = 64.76, b = 36.23, c = 70.96 Å, α = γ = 90, β = 109.4°. Analysis of the packing density shows that the asymmetric unit contains one CaM‐OLFp hybrid molecule with a solvent content of 36.42%.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>16511158</pmid><doi>10.1107/S1744309105023006</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals ANODES Calmodulin - chemistry calmodulin-binding domains calmodulin-OLFp hybrid molecule Chickens CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY CRYSTALLIZATION Crystallization Communications Crystallography, X-Ray CRYSTALS Cyclic Nucleotide-Gated Cation Channels DENSITY DIFFUSION HYBRIDIZATION Ion Channels - chemistry IONS MOLECULES Recombinant Fusion Proteins - chemistry RESOLUTION SOLVENTS SPACE GROUPS STOWING WAVELENGTHS |
title | Purification, crystallization and preliminary crystallographic studies of a calmodulin-OLFp hybrid molecule |
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