Crystals of Protein L30 from the 50 S Ribosomal Subunit of Thermus thermophilus: Preliminary Crystallographic Data
Crystals have been obtained of protein L30 from the large ribosomal subunit of an extreme thermophile, Thermus thermophilus, using ammonium sulphate as a precipitant. The crystals belong to space group P3112 with cell parameters a = b = 64·2 Å, c = 78·3 Å. They diffract X-rays to at least 2·3 Å reso...
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Veröffentlicht in: | Journal of molecular biology 1993-04, Vol.230 (4), p.1309-1310 |
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container_title | Journal of molecular biology |
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creator | Shikaeva, O.S. Sedelnikova, S.E. Fomenkova, N.P. Nikonov, S.V. Garber, M.B. |
description | Crystals have been obtained of protein L30 from the large ribosomal subunit of an extreme thermophile, Thermus thermophilus, using ammonium sulphate as a precipitant. The crystals belong to space group P3112 with cell parameters a = b = 64·2 Å, c = 78·3 Å. They diffract X-rays to at least 2·3 Å resolution. |
doi_str_mv | 10.1006/jmbi.1993.1245 |
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The crystals belong to space group P3112 with cell parameters a = b = 64·2 Å, c = 78·3 Å. 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The crystals belong to space group P3112 with cell parameters a = b = 64·2 Å, c = 78·3 Å. They diffract X-rays to at least 2·3 Å resolution.</description><subject>Crystallization</subject><subject>crystals</subject><subject>L30</subject><subject>ribosomal protein</subject><subject>Ribosomal Proteins - chemistry</subject><subject>Thermus thermophilus</subject><subject>Thermus thermophilus - chemistry</subject><subject>X-ray analysis</subject><subject>X-Ray Diffraction</subject><issn>0022-2836</issn><issn>1089-8638</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFr3DAQRkVpSbZJr7kFdCi9eSNZkiXlVrZJG1hoSdKzkOVRVsGyNpJdyL-vTUyvPc3he7xh5kPogpItJaS5eo5t2FKt2ZbWXLxDG0qUrlTD1Hu0IaSuq1qx5hR9LOWZECIYVyfoRHElGVEblHf5tYy2Lzh5_CunEcKA94xgn1PE4wGwIPgB34c2lRRtjx-mdhrCuOCPB8hxKguVYzoeQj-V61kCfYhhsPkVr_I-PWU75w5_s6M9Rx_8vBA-rfMM_b69edz9qPY_v9_tvu4rYFSMFchGNkJ01jLO2671vCa2o0yC09QDcKEkV9oJ8F47rj3RUBNprRMaRMfYGfry5j3m9DJBGU0MxUHf2wHSVIwUkgpd6_-CtFFSUVbP4OUKTm2EzhxziPOZZv3mnH9ec1uc7X22gwvlH8Yl45IsGvWGwXz9nwDZFBdgcNCFDG40XQqGErPUa5Z6zVKvWeplfwH0L5d-</recordid><startdate>19930420</startdate><enddate>19930420</enddate><creator>Shikaeva, O.S.</creator><creator>Sedelnikova, S.E.</creator><creator>Fomenkova, N.P.</creator><creator>Nikonov, S.V.</creator><creator>Garber, M.B.</creator><general>Elsevier Ltd</general><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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19930420</creationdate><title>Crystals of Protein L30 from the 50 S Ribosomal Subunit of Thermus thermophilus: Preliminary Crystallographic Data</title><author>Shikaeva, O.S. ; Sedelnikova, S.E. ; Fomenkova, N.P. ; Nikonov, S.V. ; Garber, M.B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e315t-e767655daa344bdbf420ad137ec91fee4587489c5eff9c49f09e207aac59e5d33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Crystallization</topic><topic>crystals</topic><topic>L30</topic><topic>ribosomal protein</topic><topic>Ribosomal Proteins - chemistry</topic><topic>Thermus thermophilus</topic><topic>Thermus thermophilus - chemistry</topic><topic>X-ray analysis</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Shikaeva, O.S.</creatorcontrib><creatorcontrib>Sedelnikova, S.E.</creatorcontrib><creatorcontrib>Fomenkova, N.P.</creatorcontrib><creatorcontrib>Nikonov, S.V.</creatorcontrib><creatorcontrib>Garber, M.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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Shikaeva, O.S.</au><au>Sedelnikova, S.E.</au><au>Fomenkova, N.P.</au><au>Nikonov, S.V.</au><au>Garber, M.B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystals of Protein L30 from the 50 S Ribosomal Subunit of Thermus thermophilus: Preliminary Crystallographic Data</atitle><jtitle>Journal of molecular biology</jtitle><addtitle>J Mol Biol</addtitle><date>1993-04-20</date><risdate>1993</risdate><volume>230</volume><issue>4</issue><spage>1309</spage><epage>1310</epage><pages>1309-1310</pages><issn>0022-2836</issn><eissn>1089-8638</eissn><coden>JMOBAK</coden><abstract>Crystals have been obtained of protein L30 from the large ribosomal subunit of an extreme thermophile, Thermus thermophilus, using ammonium sulphate as a precipitant. The crystals belong to space group P3112 with cell parameters a = b = 64·2 Å, c = 78·3 Å. They diffract X-rays to at least 2·3 Å resolution.</abstract><cop>Oxford</cop><pub>Elsevier Ltd</pub><pmid>8487308</pmid><doi>10.1006/jmbi.1993.1245</doi><tpages>2</tpages></addata></record> |
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source | MEDLINE; Elsevier ScienceDirect Journals Complete |
subjects | Crystallization crystals L30 ribosomal protein Ribosomal Proteins - chemistry Thermus thermophilus Thermus thermophilus - chemistry X-ray analysis X-Ray Diffraction |
title | Crystals of Protein L30 from the 50 S Ribosomal Subunit of Thermus thermophilus: Preliminary Crystallographic Data |
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