Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein
The nucleotide-binding domain of the Na,K-ATPase ion pump was expressed with a His tag in Escherichia coli and purified. The soluble 24 kDa derivative consists of 214 amino-acid residues and was crystallized in the presence of NiCl(2). The crystals belong to space group F23, with unit-cell parameter...
Gespeichert in:
| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2003-07, Vol.59 (Pt 7), p.1259-1261 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1261 |
|---|---|
| container_issue | Pt 7 |
| container_start_page | 1259 |
| container_title | Acta crystallographica. Section D, Biological crystallography. |
| container_volume | 59 |
| creator | Haue, Lisbeth Pedersen, Per A Jorgensen, Peter L Håkansson, Kjell O |
| description | The nucleotide-binding domain of the Na,K-ATPase ion pump was expressed with a His tag in Escherichia coli and purified. The soluble 24 kDa derivative consists of 214 amino-acid residues and was crystallized in the presence of NiCl(2). The crystals belong to space group F23, with unit-cell parameters a = b = c = 147.5 A, and diffract to 3.1 A. Complete data sets could be collected from native and thimerosal-treated crystals frozen in 50% sucrose. Five mercury positions were found and initial SIR phases calculated. |
| doi_str_mv | 10.1107/S0907444903008795 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_73463440</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>73463440</sourcerecordid><originalsourceid>FETCH-LOGICAL-p139t-9f9fd998f0aed64fb3eb5ae343173152a88cfa78d3b58a94c37b086b5313d1ae3</originalsourceid><addsrcrecordid>eNo1kMtOwzAQRb0A0VL4ADbIKwRSA3bs1PayqniJqiBR1tU4salR4gQ7kSjfwEeT0rIazdHR3NFF6IySa0qJuHkligjOuSKMEClUdoCGW5Rs2QAdx_hBCElTJo7QgKaSpULIIfqZlbV3_n2MzVcTTIyu9mPcdMFZl0Pbbxh8gfOwiS2Upfvesdridm3wIinqCpzHNtTVH4GyWcNleoVjpzvv2n-zMpUO4E0SG_DbQLyA8VMyXb5ANLgJdWucP0GHFspoTvdzhN7ubpezh2T-fP84m86ThjLVJsoqWyglLQFTTLjVzOgMDOOMCkazFKTMLQhZMJ1JUDxnQhM50RmjrKC9OEIXu7t97mdnYruqXMxNWfYP1l1cCcYnjHPSi-d7sdOVKVZNcBWEzeq_P_YLs71yfw</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>73463440</pqid></control><display><type>article</type><title>Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Alma/SFX Local Collection</source><creator>Haue, Lisbeth ; Pedersen, Per A ; Jorgensen, Peter L ; Håkansson, Kjell O</creator><creatorcontrib>Haue, Lisbeth ; Pedersen, Per A ; Jorgensen, Peter L ; Håkansson, Kjell O</creatorcontrib><description>The nucleotide-binding domain of the Na,K-ATPase ion pump was expressed with a His tag in Escherichia coli and purified. The soluble 24 kDa derivative consists of 214 amino-acid residues and was crystallized in the presence of NiCl(2). The crystals belong to space group F23, with unit-cell parameters a = b = c = 147.5 A, and diffract to 3.1 A. Complete data sets could be collected from native and thimerosal-treated crystals frozen in 50% sucrose. Five mercury positions were found and initial SIR phases calculated.</description><identifier>ISSN: 0907-4449</identifier><identifier>DOI: 10.1107/S0907444903008795</identifier><identifier>PMID: 12832778</identifier><language>eng</language><publisher>United States</publisher><subject>Amino Acid Sequence ; Animals ; Binding Sites ; Cloning, Molecular ; Crystallization - methods ; Membrane Proteins - chemistry ; Nickel ; Protein Structure, Tertiary ; Protein Subunits - chemistry ; Sodium-Potassium-Exchanging ATPase - chemistry ; Swine ; Thimerosal ; X-Ray Diffraction - methods</subject><ispartof>Acta crystallographica. Section D, Biological crystallography., 2003-07, Vol.59 (Pt 7), p.1259-1261</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12832778$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Haue, Lisbeth</creatorcontrib><creatorcontrib>Pedersen, Per A</creatorcontrib><creatorcontrib>Jorgensen, Peter L</creatorcontrib><creatorcontrib>Håkansson, Kjell O</creatorcontrib><title>Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein</title><title>Acta crystallographica. Section D, Biological crystallography.</title><addtitle>Acta Crystallogr D Biol Crystallogr</addtitle><description>The nucleotide-binding domain of the Na,K-ATPase ion pump was expressed with a His tag in Escherichia coli and purified. The soluble 24 kDa derivative consists of 214 amino-acid residues and was crystallized in the presence of NiCl(2). The crystals belong to space group F23, with unit-cell parameters a = b = c = 147.5 A, and diffract to 3.1 A. Complete data sets could be collected from native and thimerosal-treated crystals frozen in 50% sucrose. Five mercury positions were found and initial SIR phases calculated.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Cloning, Molecular</subject><subject>Crystallization - methods</subject><subject>Membrane Proteins - chemistry</subject><subject>Nickel</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Subunits - chemistry</subject><subject>Sodium-Potassium-Exchanging ATPase - chemistry</subject><subject>Swine</subject><subject>Thimerosal</subject><subject>X-Ray Diffraction - methods</subject><issn>0907-4449</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1kMtOwzAQRb0A0VL4ADbIKwRSA3bs1PayqniJqiBR1tU4salR4gQ7kSjfwEeT0rIazdHR3NFF6IySa0qJuHkligjOuSKMEClUdoCGW5Rs2QAdx_hBCElTJo7QgKaSpULIIfqZlbV3_n2MzVcTTIyu9mPcdMFZl0Pbbxh8gfOwiS2Upfvesdridm3wIinqCpzHNtTVH4GyWcNleoVjpzvv2n-zMpUO4E0SG_DbQLyA8VMyXb5ANLgJdWucP0GHFspoTvdzhN7ubpezh2T-fP84m86ThjLVJsoqWyglLQFTTLjVzOgMDOOMCkazFKTMLQhZMJ1JUDxnQhM50RmjrKC9OEIXu7t97mdnYruqXMxNWfYP1l1cCcYnjHPSi-d7sdOVKVZNcBWEzeq_P_YLs71yfw</recordid><startdate>200307</startdate><enddate>200307</enddate><creator>Haue, Lisbeth</creator><creator>Pedersen, Per A</creator><creator>Jorgensen, Peter L</creator><creator>Håkansson, Kjell O</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>200307</creationdate><title>Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein</title><author>Haue, Lisbeth ; Pedersen, Per A ; Jorgensen, Peter L ; Håkansson, Kjell O</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p139t-9f9fd998f0aed64fb3eb5ae343173152a88cfa78d3b58a94c37b086b5313d1ae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Cloning, Molecular</topic><topic>Crystallization - methods</topic><topic>Membrane Proteins - chemistry</topic><topic>Nickel</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Subunits - chemistry</topic><topic>Sodium-Potassium-Exchanging ATPase - chemistry</topic><topic>Swine</topic><topic>Thimerosal</topic><topic>X-Ray Diffraction - methods</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Haue, Lisbeth</creatorcontrib><creatorcontrib>Pedersen, Per A</creatorcontrib><creatorcontrib>Jorgensen, Peter L</creatorcontrib><creatorcontrib>Håkansson, Kjell O</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Haue, Lisbeth</au><au>Pedersen, Per A</au><au>Jorgensen, Peter L</au><au>Håkansson, Kjell O</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><addtitle>Acta Crystallogr D Biol Crystallogr</addtitle><date>2003-07</date><risdate>2003</risdate><volume>59</volume><issue>Pt 7</issue><spage>1259</spage><epage>1261</epage><pages>1259-1261</pages><issn>0907-4449</issn><abstract>The nucleotide-binding domain of the Na,K-ATPase ion pump was expressed with a His tag in Escherichia coli and purified. The soluble 24 kDa derivative consists of 214 amino-acid residues and was crystallized in the presence of NiCl(2). The crystals belong to space group F23, with unit-cell parameters a = b = c = 147.5 A, and diffract to 3.1 A. Complete data sets could be collected from native and thimerosal-treated crystals frozen in 50% sucrose. Five mercury positions were found and initial SIR phases calculated.</abstract><cop>United States</cop><pmid>12832778</pmid><doi>10.1107/S0907444903008795</doi><tpages>3</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0907-4449 |
| ispartof | Acta crystallographica. Section D, Biological crystallography., 2003-07, Vol.59 (Pt 7), p.1259-1261 |
| issn | 0907-4449 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_73463440 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Binding Sites Cloning, Molecular Crystallization - methods Membrane Proteins - chemistry Nickel Protein Structure, Tertiary Protein Subunits - chemistry Sodium-Potassium-Exchanging ATPase - chemistry Swine Thimerosal X-Ray Diffraction - methods |
| title | Cloning, expression, purification and crystallization of the N-domain from the alpha(2) subunit of the membrane-spanning Na,K-ATPase protein |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-20T17%3A50%3A37IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Cloning,%20expression,%20purification%20and%20crystallization%20of%20the%20N-domain%20from%20the%20alpha(2)%20subunit%20of%20the%20membrane-spanning%20Na,K-ATPase%20protein&rft.jtitle=Acta%20crystallographica.%20Section%20D,%20Biological%20crystallography.&rft.au=Haue,%20Lisbeth&rft.date=2003-07&rft.volume=59&rft.issue=Pt%207&rft.spage=1259&rft.epage=1261&rft.pages=1259-1261&rft.issn=0907-4449&rft_id=info:doi/10.1107/S0907444903008795&rft_dat=%3Cproquest_pubme%3E73463440%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=73463440&rft_id=info:pmid/12832778&rfr_iscdi=true |