Overexpression, crystallization and preliminary X-ray crystallographic analysis of the C-terminal cytosolic domain of mouse anoctamin 1
Transmembrane protein 16A (TMEM16A, also known as anoctamin 1; ANO1) is a bona fide Ca2+‐activated chloride channel that is activated by intracellular Ca2+‐ and Ca2+‐mobilizing stimuli and plays important roles in a variety of physiological functions. To elucidate the structural features of ANO1, st...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2011-10, Vol.67 (10), p.1250-1252 |
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| container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
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| creator | Park, Sang Ho Chung, Ho Kyung Kim, Do Jin Han, Mi Ra Park, Mi Seul Oh, Uhtaek Kim, Hyun-Jung Han, Byung Woo |
| description | Transmembrane protein 16A (TMEM16A, also known as anoctamin 1; ANO1) is a bona fide Ca2+‐activated chloride channel that is activated by intracellular Ca2+‐ and Ca2+‐mobilizing stimuli and plays important roles in a variety of physiological functions. To elucidate the structural features of ANO1, structural analysis of the C‐terminal cytosolic domain of mouse ANO1 (mANO1‐CTD) was initiated. mANO1‐CTD was overexpressed in Escherichia coli and was crystallized at 297 K using a reservoir solution consisting of 0.2 M sodium acetate trihydrate, 0.1 M Tris–HCl pH 8.5 and 30%(w/v) PEG 4000. X‐ray diffraction data were collected to 2.3 Å resolution. The crystals belonged to the orthorhombic space group P212121, with unit‐cell parameters a = 73.96, b = 103.73, c = 114.71 Å. If it is assumed that eight copies of a monomer molecule are present in the crystallographic asymmetric unit, the crystal volume per protein mass (VM) is 2.38 Å3 Da−1 and the solvent content is 48.38%. Attempts to solve the structure of mANO1‐CTD by the MAD method using selenomethionine‐labelled mANO1‐CTD or heavy‐atom‐derivatized crystals are in progress. |
| doi_str_mv | 10.1107/S1744309111027989 |
| format | Article |
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To elucidate the structural features of ANO1, structural analysis of the C‐terminal cytosolic domain of mouse ANO1 (mANO1‐CTD) was initiated. mANO1‐CTD was overexpressed in Escherichia coli and was crystallized at 297 K using a reservoir solution consisting of 0.2 M sodium acetate trihydrate, 0.1 M Tris–HCl pH 8.5 and 30%(w/v) PEG 4000. X‐ray diffraction data were collected to 2.3 Å resolution. The crystals belonged to the orthorhombic space group P212121, with unit‐cell parameters a = 73.96, b = 103.73, c = 114.71 Å. If it is assumed that eight copies of a monomer molecule are present in the crystallographic asymmetric unit, the crystal volume per protein mass (VM) is 2.38 Å3 Da−1 and the solvent content is 48.38%. Attempts to solve the structure of mANO1‐CTD by the MAD method using selenomethionine‐labelled mANO1‐CTD or heavy‐atom‐derivatized crystals are in progress.</description><identifier>ISSN: 1744-3091</identifier><identifier>EISSN: 1744-3091</identifier><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S1744309111027989</identifier><identifier>PMID: 22102040</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Animals ; Anoctamin-1 ; Channels ; chloride channels ; Chloride Channels - chemistry ; Chlorides ; Crystallization ; Crystallization Communications ; Crystallography ; Crystallography, X-Ray ; Crystals ; Cytosol - chemistry ; Gene Expression ; Mice ; Proteins ; Reproduction ; transmembrane protein 16A ; X-rays</subject><ispartof>Acta crystallographica. Section F, Structural biology and crystallization communications, 2011-10, Vol.67 (10), p.1250-1252</ispartof><rights>Park et al. 2011</rights><rights>2011 International Union of Crystallography. All rights reserved.</rights><rights>Park et al. 2011</rights><rights>Park et al. 2011 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5479-cd834fec95d2fa8427bbbd2ecc71c320506a46cc042a0773ebfd6ffe4f871db03</citedby><cites>FETCH-LOGICAL-c5479-cd834fec95d2fa8427bbbd2ecc71c320506a46cc042a0773ebfd6ffe4f871db03</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3212375/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3212375/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,725,778,782,883,1414,27907,27908,45557,45558,53774,53776</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22102040$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Park, Sang Ho</creatorcontrib><creatorcontrib>Chung, Ho Kyung</creatorcontrib><creatorcontrib>Kim, Do Jin</creatorcontrib><creatorcontrib>Han, Mi Ra</creatorcontrib><creatorcontrib>Park, Mi Seul</creatorcontrib><creatorcontrib>Oh, Uhtaek</creatorcontrib><creatorcontrib>Kim, Hyun-Jung</creatorcontrib><creatorcontrib>Han, Byung Woo</creatorcontrib><title>Overexpression, crystallization and preliminary X-ray crystallographic analysis of the C-terminal cytosolic domain of mouse anoctamin 1</title><title>Acta crystallographica. Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><description>Transmembrane protein 16A (TMEM16A, also known as anoctamin 1; ANO1) is a bona fide Ca2+‐activated chloride channel that is activated by intracellular Ca2+‐ and Ca2+‐mobilizing stimuli and plays important roles in a variety of physiological functions. To elucidate the structural features of ANO1, structural analysis of the C‐terminal cytosolic domain of mouse ANO1 (mANO1‐CTD) was initiated. mANO1‐CTD was overexpressed in Escherichia coli and was crystallized at 297 K using a reservoir solution consisting of 0.2 M sodium acetate trihydrate, 0.1 M Tris–HCl pH 8.5 and 30%(w/v) PEG 4000. X‐ray diffraction data were collected to 2.3 Å resolution. The crystals belonged to the orthorhombic space group P212121, with unit‐cell parameters a = 73.96, b = 103.73, c = 114.71 Å. If it is assumed that eight copies of a monomer molecule are present in the crystallographic asymmetric unit, the crystal volume per protein mass (VM) is 2.38 Å3 Da−1 and the solvent content is 48.38%. Attempts to solve the structure of mANO1‐CTD by the MAD method using selenomethionine‐labelled mANO1‐CTD or heavy‐atom‐derivatized crystals are in progress.</description><subject>Animals</subject><subject>Anoctamin-1</subject><subject>Channels</subject><subject>chloride channels</subject><subject>Chloride Channels - chemistry</subject><subject>Chlorides</subject><subject>Crystallization</subject><subject>Crystallization Communications</subject><subject>Crystallography</subject><subject>Crystallography, X-Ray</subject><subject>Crystals</subject><subject>Cytosol - chemistry</subject><subject>Gene Expression</subject><subject>Mice</subject><subject>Proteins</subject><subject>Reproduction</subject><subject>transmembrane protein 16A</subject><subject>X-rays</subject><issn>1744-3091</issn><issn>1744-3091</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFks9u1DAQxiMEoqXwAFxQJA5wIDD-kzi5IFWr7m5FRZEAFU6W40y6Lk68tbOl4QV47Trasiogwcnjmd_3aWY0SfKUwGtCQLz5SATnDCoSf1RUZXUv2Z9S2ZS7fyfeSx6FcAHAWFWUD5M9SqMAOOwnP0-v0OP12mMIxvWvUu3HMChrzQ81xESq-iaNVWs60ys_pl8yr8Yd5c69Wq-MjpiyYzAhdW06rDCdZQP6SWJTPQ4uOBuhxnXK9BPSuU3AKHJ6UJFKyePkQatswCe370HyeX70abbMTk4Xx7PDk0znXFSZbkrGW9RV3tBWlZyKuq4biloLohmFHArFC62BUwVCMKzbpmhb5G0pSFMDO0jebn3Xm7rDRmM_eGXl2psuTiedMvL3Sm9W8txdSUYJZSKPBi9uDby73GAYZGeCRmtVj3EoWUFeiJKCiOTLf5KkEISzEmDq6vkf6IXb-Li8SAlGCqCckkiRLaW9C8Fju2ubgJwOQv51EFHz7O68O8WvC4hAtQW-G4vj_x3l4dc5nZ_ljEzm2VZrwoDXO63y32Qh4rLk2fuFXMA7Nl9-WMqK3QCbm9OT</recordid><startdate>201110</startdate><enddate>201110</enddate><creator>Park, Sang Ho</creator><creator>Chung, Ho Kyung</creator><creator>Kim, Do Jin</creator><creator>Han, Mi Ra</creator><creator>Park, Mi Seul</creator><creator>Oh, Uhtaek</creator><creator>Kim, Hyun-Jung</creator><creator>Han, Byung Woo</creator><general>International Union of Crystallography</general><general>Wiley Subscription Services, Inc</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>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>7U5</scope><scope>L7M</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>201110</creationdate><title>Overexpression, crystallization and preliminary X-ray crystallographic analysis of the C-terminal cytosolic domain of mouse anoctamin 1</title><author>Park, Sang Ho ; Chung, Ho Kyung ; Kim, Do Jin ; Han, Mi Ra ; Park, Mi Seul ; Oh, Uhtaek ; Kim, Hyun-Jung ; Han, Byung Woo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5479-cd834fec95d2fa8427bbbd2ecc71c320506a46cc042a0773ebfd6ffe4f871db03</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Animals</topic><topic>Anoctamin-1</topic><topic>Channels</topic><topic>chloride channels</topic><topic>Chloride Channels - chemistry</topic><topic>Chlorides</topic><topic>Crystallization</topic><topic>Crystallization Communications</topic><topic>Crystallography</topic><topic>Crystallography, X-Ray</topic><topic>Crystals</topic><topic>Cytosol - chemistry</topic><topic>Gene Expression</topic><topic>Mice</topic><topic>Proteins</topic><topic>Reproduction</topic><topic>transmembrane protein 16A</topic><topic>X-rays</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Park, Sang Ho</creatorcontrib><creatorcontrib>Chung, Ho Kyung</creatorcontrib><creatorcontrib>Kim, Do Jin</creatorcontrib><creatorcontrib>Han, Mi Ra</creatorcontrib><creatorcontrib>Park, Mi Seul</creatorcontrib><creatorcontrib>Oh, Uhtaek</creatorcontrib><creatorcontrib>Kim, Hyun-Jung</creatorcontrib><creatorcontrib>Han, Byung Woo</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>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>MEDLINE - Academic</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>Park, Sang Ho</au><au>Chung, Ho Kyung</au><au>Kim, Do Jin</au><au>Han, Mi Ra</au><au>Park, Mi Seul</au><au>Oh, Uhtaek</au><au>Kim, Hyun-Jung</au><au>Han, Byung Woo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Overexpression, crystallization and preliminary X-ray crystallographic analysis of the C-terminal cytosolic domain of mouse anoctamin 1</atitle><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle><addtitle>Acta Cryst. F</addtitle><date>2011-10</date><risdate>2011</risdate><volume>67</volume><issue>10</issue><spage>1250</spage><epage>1252</epage><pages>1250-1252</pages><issn>1744-3091</issn><eissn>1744-3091</eissn><eissn>2053-230X</eissn><abstract>Transmembrane protein 16A (TMEM16A, also known as anoctamin 1; ANO1) is a bona fide Ca2+‐activated chloride channel that is activated by intracellular Ca2+‐ and Ca2+‐mobilizing stimuli and plays important roles in a variety of physiological functions. To elucidate the structural features of ANO1, structural analysis of the C‐terminal cytosolic domain of mouse ANO1 (mANO1‐CTD) was initiated. mANO1‐CTD was overexpressed in Escherichia coli and was crystallized at 297 K using a reservoir solution consisting of 0.2 M sodium acetate trihydrate, 0.1 M Tris–HCl pH 8.5 and 30%(w/v) PEG 4000. X‐ray diffraction data were collected to 2.3 Å resolution. The crystals belonged to the orthorhombic space group P212121, with unit‐cell parameters a = 73.96, b = 103.73, c = 114.71 Å. If it is assumed that eight copies of a monomer molecule are present in the crystallographic asymmetric unit, the crystal volume per protein mass (VM) is 2.38 Å3 Da−1 and the solvent content is 48.38%. Attempts to solve the structure of mANO1‐CTD by the MAD method using selenomethionine‐labelled mANO1‐CTD or heavy‐atom‐derivatized crystals are in progress.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>22102040</pmid><doi>10.1107/S1744309111027989</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Animals Anoctamin-1 Channels chloride channels Chloride Channels - chemistry Chlorides Crystallization Crystallization Communications Crystallography Crystallography, X-Ray Crystals Cytosol - chemistry Gene Expression Mice Proteins Reproduction transmembrane protein 16A X-rays |
| title | Overexpression, crystallization and preliminary X-ray crystallographic analysis of the C-terminal cytosolic domain of mouse anoctamin 1 |
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