Crystallization and preliminary X-ray investigation of recombinant human interleukin 10
Crystals of recombinant human interleukin 10 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space group P41212 or P43212; the unit cell axes are a = 36.5 Å and c = 221.9 Å. There is the equivalent of one polypeptide chain in the asymmetric unit. The crystals are sta...
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| Veröffentlicht in: | Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 1995-06, Vol.22 (2), p.187-190 |
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| container_end_page | 190 |
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| container_title | Proteins, structure, function, and bioinformatics |
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| creator | Cook, William J. Windsor, William T. Murgolo, Nicholas J. Tindall, Stephen H. Nagabhushan, Tattanahalli L. Walter, Mark R. |
| description | Crystals of recombinant human interleukin 10 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space group P41212 or P43212; the unit cell axes are a = 36.5 Å and c = 221.9 Å. There is the equivalent of one polypeptide chain in the asymmetric unit. The crystals are stable to X‐rays and diffract to at least 2.5 Å resolution. © 1995 Wiley‐Liss, Inc. |
| doi_str_mv | 10.1002/prot.340220211 |
| format | Article |
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The crystals are tetragonal, space group P41212 or P43212; the unit cell axes are a = 36.5 Å and c = 221.9 Å. There is the equivalent of one polypeptide chain in the asymmetric unit. The crystals are stable to X‐rays and diffract to at least 2.5 Å resolution. © 1995 Wiley‐Liss, Inc.</description><identifier>ISSN: 0887-3585</identifier><identifier>EISSN: 1097-0134</identifier><identifier>DOI: 10.1002/prot.340220211</identifier><identifier>PMID: 7567966</identifier><language>eng</language><publisher>Hoboken: Wiley Subscription Services, Inc., A Wiley Company</publisher><subject>Ammonium Sulfate - chemistry ; Animals ; BCRF1 ; CHO Cells - metabolism ; Cricetinae ; crystal seeding ; cytokine ; Escherichia coli - metabolism ; Humans ; Interleukin-10 - chemistry ; protein structure ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; X-Ray Diffraction</subject><ispartof>Proteins, structure, function, and bioinformatics, 1995-06, Vol.22 (2), p.187-190</ispartof><rights>Copyright © 1995 Wiley‐Liss, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c3331-48b008b89a630a442bf2c766911cb9378b2ae535a50d8c8dd39e6fa113c2a8e83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fprot.340220211$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fprot.340220211$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27901,27902,45550,45551</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7567966$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Cook, William J.</creatorcontrib><creatorcontrib>Windsor, William T.</creatorcontrib><creatorcontrib>Murgolo, Nicholas J.</creatorcontrib><creatorcontrib>Tindall, Stephen H.</creatorcontrib><creatorcontrib>Nagabhushan, Tattanahalli L.</creatorcontrib><creatorcontrib>Walter, Mark R.</creatorcontrib><title>Crystallization and preliminary X-ray investigation of recombinant human interleukin 10</title><title>Proteins, structure, function, and bioinformatics</title><addtitle>Proteins</addtitle><description>Crystals of recombinant human interleukin 10 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space group P41212 or P43212; the unit cell axes are a = 36.5 Å and c = 221.9 Å. There is the equivalent of one polypeptide chain in the asymmetric unit. The crystals are stable to X‐rays and diffract to at least 2.5 Å resolution. © 1995 Wiley‐Liss, Inc.</description><subject>Ammonium Sulfate - chemistry</subject><subject>Animals</subject><subject>BCRF1</subject><subject>CHO Cells - metabolism</subject><subject>Cricetinae</subject><subject>crystal seeding</subject><subject>cytokine</subject><subject>Escherichia coli - metabolism</subject><subject>Humans</subject><subject>Interleukin-10 - chemistry</subject><subject>protein structure</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - chemistry</subject><subject>X-Ray Diffraction</subject><issn>0887-3585</issn><issn>1097-0134</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkD1PwzAQhi0EKqWwsiFlYks5x4k_RlTRgoRohUBFXSwnccCQj2InQPn1GKWq2JhuuOd9dfcgdIphjAGii7Vt2jGJIYogwngPDTEIFgIm8T4aAucsJAlPDtGRc68AQAWhAzRgCWWC0iFaTuzGtaoszbdqTVMHqs6DtdWlqUyt7CZ4Cq3aBKb-0K41zz3TFIHVWVOlHqnb4KWrVO2RVttSd2-mDjAco4NClU6fbOcIPU6vHibX4e18djO5vA0zQggOY54C8JQLRQmoOI7SIsoYpQLjLBWE8TRSOiGJSiDnGc9zIjQtFMYkixTXnIzQed_rPbx3_kZZGZfpslS1bjonGUt8FyYeHPdgZhvnrC7k2prKfygxyF-T8tek3Jn0gbNtc5dWOt_hW3V-L_r9pyn15p82ubifP_ztDvusca3-2mWVfZOUEZbI5d1MruKFiOPVVC7JD7cFkEc</recordid><startdate>199506</startdate><enddate>199506</enddate><creator>Cook, William J.</creator><creator>Windsor, William T.</creator><creator>Murgolo, Nicholas J.</creator><creator>Tindall, Stephen H.</creator><creator>Nagabhushan, Tattanahalli L.</creator><creator>Walter, Mark R.</creator><general>Wiley Subscription Services, Inc., A Wiley Company</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></search><sort><creationdate>199506</creationdate><title>Crystallization and preliminary X-ray investigation of recombinant human interleukin 10</title><author>Cook, William J. ; Windsor, William T. ; Murgolo, Nicholas J. ; Tindall, Stephen H. ; Nagabhushan, Tattanahalli L. ; Walter, Mark R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3331-48b008b89a630a442bf2c766911cb9378b2ae535a50d8c8dd39e6fa113c2a8e83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Ammonium Sulfate - chemistry</topic><topic>Animals</topic><topic>BCRF1</topic><topic>CHO Cells - metabolism</topic><topic>Cricetinae</topic><topic>crystal seeding</topic><topic>cytokine</topic><topic>Escherichia coli - metabolism</topic><topic>Humans</topic><topic>Interleukin-10 - chemistry</topic><topic>protein structure</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - chemistry</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Cook, William J.</creatorcontrib><creatorcontrib>Windsor, William T.</creatorcontrib><creatorcontrib>Murgolo, Nicholas J.</creatorcontrib><creatorcontrib>Tindall, Stephen H.</creatorcontrib><creatorcontrib>Nagabhushan, Tattanahalli L.</creatorcontrib><creatorcontrib>Walter, Mark R.</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><jtitle>Proteins, structure, function, and bioinformatics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Cook, William J.</au><au>Windsor, William T.</au><au>Murgolo, Nicholas J.</au><au>Tindall, Stephen H.</au><au>Nagabhushan, Tattanahalli L.</au><au>Walter, Mark R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary X-ray investigation of recombinant human interleukin 10</atitle><jtitle>Proteins, structure, function, and bioinformatics</jtitle><addtitle>Proteins</addtitle><date>1995-06</date><risdate>1995</risdate><volume>22</volume><issue>2</issue><spage>187</spage><epage>190</epage><pages>187-190</pages><issn>0887-3585</issn><eissn>1097-0134</eissn><abstract>Crystals of recombinant human interleukin 10 have been grown from solutions of ammonium sulfate. The crystals are tetragonal, space group P41212 or P43212; the unit cell axes are a = 36.5 Å and c = 221.9 Å. There is the equivalent of one polypeptide chain in the asymmetric unit. The crystals are stable to X‐rays and diffract to at least 2.5 Å resolution. © 1995 Wiley‐Liss, Inc.</abstract><cop>Hoboken</cop><pub>Wiley Subscription Services, Inc., A Wiley Company</pub><pmid>7567966</pmid><doi>10.1002/prot.340220211</doi><tpages>4</tpages></addata></record> |
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| ispartof | Proteins, structure, function, and bioinformatics, 1995-06, Vol.22 (2), p.187-190 |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Ammonium Sulfate - chemistry Animals BCRF1 CHO Cells - metabolism Cricetinae crystal seeding cytokine Escherichia coli - metabolism Humans Interleukin-10 - chemistry protein structure Recombinant Proteins - biosynthesis Recombinant Proteins - chemistry X-Ray Diffraction |
| title | Crystallization and preliminary X-ray investigation of recombinant human interleukin 10 |
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