Crystallization of O6-methylguanine-DNA methyltransferase from Escherichia coli
The 19,000 Mr C-terminal domain of the Escherichia coli ada gene product that contains O6-methylguanine-DNA methyltransferase DNA repair activity has been crystallized in a low-salt environment. The crystals, which diffract to 2.3 A (1 A = 0.1 nm), are suitable for detailed structural studies. The s...
Gespeichert in:
| Veröffentlicht in: | Journal of molecular biology 1988-04, Vol.200 (4), p.751-752 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 752 |
|---|---|
| container_issue | 4 |
| container_start_page | 751 |
| container_title | Journal of molecular biology |
| container_volume | 200 |
| creator | MOODY, P. C. E DEMPLE, B |
| description | The 19,000 Mr C-terminal domain of the Escherichia coli ada gene product that contains O6-methylguanine-DNA methyltransferase DNA repair activity has been crystallized in a low-salt environment. The crystals, which diffract to 2.3 A (1 A = 0.1 nm), are suitable for detailed structural studies. The space group is P21 with unit cell dimensions a = 46.3 A, b = 45.8 A, c = 46.9 A and beta = 113.3 degrees. |
| doi_str_mv | 10.1016/0022-2836(88)90488-3 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_78390736</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>78390736</sourcerecordid><originalsourceid>FETCH-LOGICAL-c1787-14d3872b6aaebcb16378ab4e997d91663d3f0a5adaf20df6f9fd53230388d92d3</originalsourceid><addsrcrecordid>eNo9kE1PGzEQhq2qiIbQfwDSHirUHpbaOxt79hgFKEgRucDZmvUHMdoPau8ewq_vpolyGmnmeV-NHsauBL8VXMjfnBdFXiDIn4i_Kl4i5vCFzQTHKkcJ-JXNTsg3dpHSO-d8ASWes3Pg5QIKNWObVdylgZomfNIQ-i7rfbaReeuG7a55G6kLncvvnpfZYTNE6pJ3kZLLfOzb7D6ZrYvBbANlpm_CJTvz1CT3_Tjn7PXh_mX1mK83f55Wy3VuhEKVi9ICqqKWRK42tZCgkOrSVZWylZASLHhOC7LkC2699JW308PAAdFWhYU5uzn0fsT-7-jSoNuQjGsa6lw_Jq0QKq5ATmB5AE3sU4rO648YWoo7Lbjee9R7SXovSSPq_x41TLHrY_9Yt86eQkdx0_3H8U7JUOMnLyakE6ZkseClhH854Hr-</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>78390736</pqid></control><display><type>article</type><title>Crystallization of O6-methylguanine-DNA methyltransferase from Escherichia coli</title><source>Elsevier ScienceDirect Journals Complete - AutoHoldings</source><source>MEDLINE</source><creator>MOODY, P. C. E ; DEMPLE, B</creator><creatorcontrib>MOODY, P. C. E ; DEMPLE, B</creatorcontrib><description>The 19,000 Mr C-terminal domain of the Escherichia coli ada gene product that contains O6-methylguanine-DNA methyltransferase DNA repair activity has been crystallized in a low-salt environment. The crystals, which diffract to 2.3 A (1 A = 0.1 nm), are suitable for detailed structural studies. The space group is P21 with unit cell dimensions a = 46.3 A, b = 45.8 A, c = 46.9 A and beta = 113.3 degrees.</description><identifier>ISSN: 0022-2836</identifier><identifier>EISSN: 1089-8638</identifier><identifier>DOI: 10.1016/0022-2836(88)90488-3</identifier><identifier>PMID: 3045327</identifier><identifier>CODEN: JMOBAK</identifier><language>eng</language><publisher>Oxford: Elsevier</publisher><subject>Biological and medical sciences ; Crystalline structure ; Crystallization ; Escherichia coli - enzymology ; Fundamental and applied biological sciences. Psychology ; Methyltransferases ; Molecular biophysics ; O-Methylguanine-DNA Methyltransferase ; Structure in molecular biology</subject><ispartof>Journal of molecular biology, 1988-04, Vol.200 (4), p.751-752</ispartof><rights>1988 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1787-14d3872b6aaebcb16378ab4e997d91663d3f0a5adaf20df6f9fd53230388d92d3</citedby><cites>FETCH-LOGICAL-c1787-14d3872b6aaebcb16378ab4e997d91663d3f0a5adaf20df6f9fd53230388d92d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7625046$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3045327$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>MOODY, P. C. E</creatorcontrib><creatorcontrib>DEMPLE, B</creatorcontrib><title>Crystallization of O6-methylguanine-DNA methyltransferase from Escherichia coli</title><title>Journal of molecular biology</title><addtitle>J Mol Biol</addtitle><description>The 19,000 Mr C-terminal domain of the Escherichia coli ada gene product that contains O6-methylguanine-DNA methyltransferase DNA repair activity has been crystallized in a low-salt environment. The crystals, which diffract to 2.3 A (1 A = 0.1 nm), are suitable for detailed structural studies. The space group is P21 with unit cell dimensions a = 46.3 A, b = 45.8 A, c = 46.9 A and beta = 113.3 degrees.</description><subject>Biological and medical sciences</subject><subject>Crystalline structure</subject><subject>Crystallization</subject><subject>Escherichia coli - enzymology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Methyltransferases</subject><subject>Molecular biophysics</subject><subject>O-Methylguanine-DNA Methyltransferase</subject><subject>Structure in molecular biology</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kE1PGzEQhq2qiIbQfwDSHirUHpbaOxt79hgFKEgRucDZmvUHMdoPau8ewq_vpolyGmnmeV-NHsauBL8VXMjfnBdFXiDIn4i_Kl4i5vCFzQTHKkcJ-JXNTsg3dpHSO-d8ASWes3Pg5QIKNWObVdylgZomfNIQ-i7rfbaReeuG7a55G6kLncvvnpfZYTNE6pJ3kZLLfOzb7D6ZrYvBbANlpm_CJTvz1CT3_Tjn7PXh_mX1mK83f55Wy3VuhEKVi9ICqqKWRK42tZCgkOrSVZWylZASLHhOC7LkC2699JW308PAAdFWhYU5uzn0fsT-7-jSoNuQjGsa6lw_Jq0QKq5ATmB5AE3sU4rO648YWoo7Lbjee9R7SXovSSPq_x41TLHrY_9Yt86eQkdx0_3H8U7JUOMnLyakE6ZkseClhH854Hr-</recordid><startdate>19880420</startdate><enddate>19880420</enddate><creator>MOODY, P. C. E</creator><creator>DEMPLE, B</creator><general>Elsevier</general><scope>IQODW</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>19880420</creationdate><title>Crystallization of O6-methylguanine-DNA methyltransferase from Escherichia coli</title><author>MOODY, P. C. E ; DEMPLE, B</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1787-14d3872b6aaebcb16378ab4e997d91663d3f0a5adaf20df6f9fd53230388d92d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>Biological and medical sciences</topic><topic>Crystalline structure</topic><topic>Crystallization</topic><topic>Escherichia coli - enzymology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Methyltransferases</topic><topic>Molecular biophysics</topic><topic>O-Methylguanine-DNA Methyltransferase</topic><topic>Structure in molecular biology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MOODY, P. C. E</creatorcontrib><creatorcontrib>DEMPLE, B</creatorcontrib><collection>Pascal-Francis</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>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MOODY, P. C. E</au><au>DEMPLE, B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization of O6-methylguanine-DNA methyltransferase from Escherichia coli</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1988-04-20</date><risdate>1988</risdate><volume>200</volume><issue>4</issue><spage>751</spage><epage>752</epage><pages>751-752</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>The 19,000 Mr C-terminal domain of the Escherichia coli ada gene product that contains O6-methylguanine-DNA methyltransferase DNA repair activity has been crystallized in a low-salt environment. The crystals, which diffract to 2.3 A (1 A = 0.1 nm), are suitable for detailed structural studies. The space group is P21 with unit cell dimensions a = 46.3 A, b = 45.8 A, c = 46.9 A and beta = 113.3 degrees.</abstract><cop>Oxford</cop><pub>Elsevier</pub><pmid>3045327</pmid><doi>10.1016/0022-2836(88)90488-3</doi><tpages>2</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0022-2836 |
| ispartof | Journal of molecular biology, 1988-04, Vol.200 (4), p.751-752 |
| issn | 0022-2836 1089-8638 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_78390736 |
| source | Elsevier ScienceDirect Journals Complete - AutoHoldings; MEDLINE |
| subjects | Biological and medical sciences Crystalline structure Crystallization Escherichia coli - enzymology Fundamental and applied biological sciences. Psychology Methyltransferases Molecular biophysics O-Methylguanine-DNA Methyltransferase Structure in molecular biology |
| title | Crystallization of O6-methylguanine-DNA methyltransferase from Escherichia coli |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-08T08%3A58%3A35IST&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%20of%20O6-methylguanine-DNA%20methyltransferase%20from%20Escherichia%20coli&rft.jtitle=Journal%20of%20molecular%20biology&rft.au=MOODY,%20P.%20C.%20E&rft.date=1988-04-20&rft.volume=200&rft.issue=4&rft.spage=751&rft.epage=752&rft.pages=751-752&rft.issn=0022-2836&rft.eissn=1089-8638&rft.coden=JMOBAK&rft_id=info:doi/10.1016/0022-2836(88)90488-3&rft_dat=%3Cproquest_cross%3E78390736%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=78390736&rft_id=info:pmid/3045327&rfr_iscdi=true |