Purification, crystallization and preliminary X-ray diffraction analysis of the Kelch-like motif region of mouse Keap1
Keap1 (Kelch‐like ECH‐associating protein 1) is a negative regulator of the Nrf2 transcription factor in the cytoplasm. The Kelch/DGR (double‐glycine repeat) domain of Keap1 associates with Nrf2 as well as with actin filaments. A recombinant protein containing both the Kelch/DGR domain and the C‐te...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2005-01, Vol.61 (1), p.153-155 |
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| container_title | Acta crystallographica. Section F, Structural biology and crystallization communications |
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| creator | Padmanabhan, Balasundaram Scharlock, Maria Tong, Kit I. Nakamura, Yoshihiro Kang, Moon-Il Kobayashi, Akira Matsumoto, Takehisa Tanaka, Akiko Yamamoto, Masayuki Yokoyama, Shigeyuki |
| description | Keap1 (Kelch‐like ECH‐associating protein 1) is a negative regulator of the Nrf2 transcription factor in the cytoplasm. The Kelch/DGR (double‐glycine repeat) domain of Keap1 associates with Nrf2 as well as with actin filaments. A recombinant protein containing both the Kelch/DGR domain and the C‐terminal region of mouse Keap1 was expressed in Escherichia coli, purified to near‐homogeneity and crystallized by the sitting‐drop vapour‐diffusion method. The crystal belongs to space group P61 or P65, with unit‐cell parameters a = b = 102.95, c = 55.21 Å, and contains one molecule in the asymmetric unit. A complete diffraction data was collected to 2.25 Å resolution using an R‐AXIS IV++ imaging plate mounted on an RA‐Micro7 Cu Kα rotating‐anode X‐ray generator. |
| doi_str_mv | 10.1107/S1744309104032506 |
| format | Article |
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The Kelch/DGR (double‐glycine repeat) domain of Keap1 associates with Nrf2 as well as with actin filaments. A recombinant protein containing both the Kelch/DGR domain and the C‐terminal region of mouse Keap1 was expressed in Escherichia coli, purified to near‐homogeneity and crystallized by the sitting‐drop vapour‐diffusion method. The crystal belongs to space group P61 or P65, with unit‐cell parameters a = b = 102.95, c = 55.21 Å, and contains one molecule in the asymmetric unit. A complete diffraction data was collected to 2.25 Å resolution using an R‐AXIS IV++ imaging plate mounted on an RA‐Micro7 Cu Kα rotating‐anode X‐ray generator.</description><identifier>ISSN: 1744-3091</identifier><identifier>EISSN: 1744-3091</identifier><identifier>DOI: 10.1107/S1744309104032506</identifier><identifier>PMID: 16508120</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers</publisher><subject>actin binding ; Actins - metabolism ; Adaptor Proteins, Signal Transducing - chemistry ; Adaptor Proteins, Signal Transducing - isolation & purification ; Adaptor Proteins, Signal Transducing - metabolism ; Animals ; ANODES ; antioxidants ; Binding Sites ; Cloning, Molecular ; CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY ; CRYSTALLIZATION ; Crystallization Communications ; CRYSTALS ; Cytoskeletal Proteins - chemistry ; Cytoskeletal Proteins - isolation & purification ; Cytoskeletal Proteins - metabolism ; DIFFUSION ; ESCHERICHIA COLI ; FILAMENTS ; GLYCINE ; Keap1 ; Kelch-Like ECH-Associated Protein 1 ; Mice ; MOLECULES ; Nrf2 ; PLATES ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - isolation & purification ; RESOLUTION ; SPACE GROUPS ; transcription factor ; X-RAY DIFFRACTION</subject><ispartof>Acta crystallographica. Section F, Structural biology and crystallization communications, 2005-01, Vol.61 (1), p.153-155</ispartof><rights>International Union of Crystallography 2005 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5791-f80bc02828b2306e5eaca0a62c3f766b5fd1e46d19d3c0fb01e4fbc9429a029f3</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/PMC1952392/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1952392/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,27924,27925,45574,45575,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16508120$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/22356083$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Padmanabhan, Balasundaram</creatorcontrib><creatorcontrib>Scharlock, Maria</creatorcontrib><creatorcontrib>Tong, Kit I.</creatorcontrib><creatorcontrib>Nakamura, Yoshihiro</creatorcontrib><creatorcontrib>Kang, Moon-Il</creatorcontrib><creatorcontrib>Kobayashi, Akira</creatorcontrib><creatorcontrib>Matsumoto, Takehisa</creatorcontrib><creatorcontrib>Tanaka, Akiko</creatorcontrib><creatorcontrib>Yamamoto, Masayuki</creatorcontrib><creatorcontrib>Yokoyama, Shigeyuki</creatorcontrib><title>Purification, crystallization and preliminary X-ray diffraction analysis of the Kelch-like motif region of mouse Keap1</title><title>Acta crystallographica. Section F, Structural biology and crystallization communications</title><addtitle>Acta Cryst. F</addtitle><description>Keap1 (Kelch‐like ECH‐associating protein 1) is a negative regulator of the Nrf2 transcription factor in the cytoplasm. The Kelch/DGR (double‐glycine repeat) domain of Keap1 associates with Nrf2 as well as with actin filaments. A recombinant protein containing both the Kelch/DGR domain and the C‐terminal region of mouse Keap1 was expressed in Escherichia coli, purified to near‐homogeneity and crystallized by the sitting‐drop vapour‐diffusion method. The crystal belongs to space group P61 or P65, with unit‐cell parameters a = b = 102.95, c = 55.21 Å, and contains one molecule in the asymmetric unit. A complete diffraction data was collected to 2.25 Å resolution using an R‐AXIS IV++ imaging plate mounted on an RA‐Micro7 Cu Kα rotating‐anode X‐ray generator.</description><subject>actin binding</subject><subject>Actins - metabolism</subject><subject>Adaptor Proteins, Signal Transducing - chemistry</subject><subject>Adaptor Proteins, Signal Transducing - isolation & purification</subject><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Animals</subject><subject>ANODES</subject><subject>antioxidants</subject><subject>Binding Sites</subject><subject>Cloning, Molecular</subject><subject>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</subject><subject>CRYSTALLIZATION</subject><subject>Crystallization Communications</subject><subject>CRYSTALS</subject><subject>Cytoskeletal Proteins - chemistry</subject><subject>Cytoskeletal Proteins - isolation & purification</subject><subject>Cytoskeletal Proteins - metabolism</subject><subject>DIFFUSION</subject><subject>ESCHERICHIA COLI</subject><subject>FILAMENTS</subject><subject>GLYCINE</subject><subject>Keap1</subject><subject>Kelch-Like ECH-Associated Protein 1</subject><subject>Mice</subject><subject>MOLECULES</subject><subject>Nrf2</subject><subject>PLATES</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - isolation & purification</subject><subject>RESOLUTION</subject><subject>SPACE GROUPS</subject><subject>transcription factor</subject><subject>X-RAY DIFFRACTION</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>eNqFkUFv1DAQhSMEoqXwA7ggS0g9ERjbsZNckNqKLoiqILWI0ovlOHbX1IkX21sIvx4vWZUiDpxsz3zvjZ-mKJ5ieIkx1K_OcF1VFFoMFVDCgN8rdjelclO7f-e-UzyK8SsApS1vHhY7mDNoMIHd4ubjOlhjlUzWjy-QClNM0jn783cBybFHq6CdHewow4QuyiAn1FtjglRbQrop2oi8QWmp0Xvt1LJ09lqjwSdrUNBXGy63B7-OG0Cu8OPigZEu6ifbc6_4dPzm_OhtefJh8e7o4KRUrG5xaRroFJCGNB2hwDXTUkmQnChqas47ZnqsK97jtqcKTAf5ZTrVVqSVQFpD94rXs-9q3Q26V3pMQTqxCnbIcYSXVvzdGe1SXPkbgVtGaEuywfPZwMdkRVQ2abVUfhy1SoIQyjg0NFP72zHBf1vrmMRgo9LOyVHn0KIGXAHDdQbxDKrgYwza3H4Fg9jsVPyz06x5djfDH8V2iRloZ-C7dXr6v6M4-HJMFhcMKM7actbamPSPW60M14LXtGbi8-lC4DN8eXh4fiou6S91oL4H</recordid><startdate>200501</startdate><enddate>200501</enddate><creator>Padmanabhan, Balasundaram</creator><creator>Scharlock, Maria</creator><creator>Tong, Kit I.</creator><creator>Nakamura, Yoshihiro</creator><creator>Kang, Moon-Il</creator><creator>Kobayashi, Akira</creator><creator>Matsumoto, Takehisa</creator><creator>Tanaka, Akiko</creator><creator>Yamamoto, Masayuki</creator><creator>Yokoyama, Shigeyuki</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>200501</creationdate><title>Purification, crystallization and preliminary X-ray diffraction analysis of the Kelch-like motif region of mouse Keap1</title><author>Padmanabhan, Balasundaram ; Scharlock, Maria ; Tong, Kit I. ; Nakamura, Yoshihiro ; Kang, Moon-Il ; Kobayashi, Akira ; Matsumoto, Takehisa ; Tanaka, Akiko ; Yamamoto, Masayuki ; Yokoyama, Shigeyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5791-f80bc02828b2306e5eaca0a62c3f766b5fd1e46d19d3c0fb01e4fbc9429a029f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>actin binding</topic><topic>Actins - metabolism</topic><topic>Adaptor Proteins, Signal Transducing - chemistry</topic><topic>Adaptor Proteins, Signal Transducing - isolation & purification</topic><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Animals</topic><topic>ANODES</topic><topic>antioxidants</topic><topic>Binding Sites</topic><topic>Cloning, Molecular</topic><topic>CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY</topic><topic>CRYSTALLIZATION</topic><topic>Crystallization Communications</topic><topic>CRYSTALS</topic><topic>Cytoskeletal Proteins - chemistry</topic><topic>Cytoskeletal Proteins - isolation & purification</topic><topic>Cytoskeletal Proteins - metabolism</topic><topic>DIFFUSION</topic><topic>ESCHERICHIA COLI</topic><topic>FILAMENTS</topic><topic>GLYCINE</topic><topic>Keap1</topic><topic>Kelch-Like ECH-Associated Protein 1</topic><topic>Mice</topic><topic>MOLECULES</topic><topic>Nrf2</topic><topic>PLATES</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - isolation & purification</topic><topic>RESOLUTION</topic><topic>SPACE GROUPS</topic><topic>transcription factor</topic><topic>X-RAY DIFFRACTION</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Padmanabhan, Balasundaram</creatorcontrib><creatorcontrib>Scharlock, Maria</creatorcontrib><creatorcontrib>Tong, Kit I.</creatorcontrib><creatorcontrib>Nakamura, Yoshihiro</creatorcontrib><creatorcontrib>Kang, Moon-Il</creatorcontrib><creatorcontrib>Kobayashi, Akira</creatorcontrib><creatorcontrib>Matsumoto, Takehisa</creatorcontrib><creatorcontrib>Tanaka, Akiko</creatorcontrib><creatorcontrib>Yamamoto, Masayuki</creatorcontrib><creatorcontrib>Yokoyama, Shigeyuki</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>Padmanabhan, Balasundaram</au><au>Scharlock, Maria</au><au>Tong, Kit I.</au><au>Nakamura, Yoshihiro</au><au>Kang, Moon-Il</au><au>Kobayashi, Akira</au><au>Matsumoto, Takehisa</au><au>Tanaka, Akiko</au><au>Yamamoto, Masayuki</au><au>Yokoyama, Shigeyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification, crystallization and preliminary X-ray diffraction analysis of the Kelch-like motif region of mouse Keap1</atitle><jtitle>Acta crystallographica. Section F, Structural biology and crystallization communications</jtitle><addtitle>Acta Cryst. F</addtitle><date>2005-01</date><risdate>2005</risdate><volume>61</volume><issue>1</issue><spage>153</spage><epage>155</epage><pages>153-155</pages><issn>1744-3091</issn><eissn>1744-3091</eissn><abstract>Keap1 (Kelch‐like ECH‐associating protein 1) is a negative regulator of the Nrf2 transcription factor in the cytoplasm. The Kelch/DGR (double‐glycine repeat) domain of Keap1 associates with Nrf2 as well as with actin filaments. A recombinant protein containing both the Kelch/DGR domain and the C‐terminal region of mouse Keap1 was expressed in Escherichia coli, purified to near‐homogeneity and crystallized by the sitting‐drop vapour‐diffusion method. The crystal belongs to space group P61 or P65, with unit‐cell parameters a = b = 102.95, c = 55.21 Å, and contains one molecule in the asymmetric unit. A complete diffraction data was collected to 2.25 Å resolution using an R‐AXIS IV++ imaging plate mounted on an RA‐Micro7 Cu Kα rotating‐anode X‐ray generator.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>16508120</pmid><doi>10.1107/S1744309104032506</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | actin binding Actins - metabolism Adaptor Proteins, Signal Transducing - chemistry Adaptor Proteins, Signal Transducing - isolation & purification Adaptor Proteins, Signal Transducing - metabolism Animals ANODES antioxidants Binding Sites Cloning, Molecular CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY CRYSTALLIZATION Crystallization Communications CRYSTALS Cytoskeletal Proteins - chemistry Cytoskeletal Proteins - isolation & purification Cytoskeletal Proteins - metabolism DIFFUSION ESCHERICHIA COLI FILAMENTS GLYCINE Keap1 Kelch-Like ECH-Associated Protein 1 Mice MOLECULES Nrf2 PLATES Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - isolation & purification RESOLUTION SPACE GROUPS transcription factor X-RAY DIFFRACTION |
| title | Purification, crystallization and preliminary X-ray diffraction analysis of the Kelch-like motif region of mouse Keap1 |
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