Preliminary X-ray crystallography studies of recombinant human interleukin-1 alpha. Purification and structural characterization
Human interleukin-1 alpha, cloned and expressed in E. coli, has been purified and structurally characterized by various physiochemical methods, including mass spectrometry. The recombinant protein has been crystallized by the hanging drop vapor diffusion method using dimethyl sulfoxide as the precip...
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| Veröffentlicht in: | The Journal of biological chemistry 1989-03, Vol.264 (9), p.4948-4952 |
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| container_issue | 9 |
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| container_title | The Journal of biological chemistry |
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| creator | Hassell, A M Johanson, K O Goodhart, P Young, P R Holskin, B P Carr, S A Roberts, G D Simon, P L Chen, M J Lewis, M |
| description | Human interleukin-1 alpha, cloned and expressed in E. coli, has been purified and structurally characterized by various physiochemical
methods, including mass spectrometry. The recombinant protein has been crystallized by the hanging drop vapor diffusion method
using dimethyl sulfoxide as the precipitating agent. The space group is P2(1)2(1)2(1). Unit cell dimensions are a = 44.1,
b = 57.1, and c = 61.7 A and alpha = beta = gamma = 90 degrees. The crystals diffract to beyond 1.7 A and are suitable for
high resolution data collection. Native diffraction data were collected. Screens for heavy atom derivatives have been initiated. |
| format | Article |
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methods, including mass spectrometry. The recombinant protein has been crystallized by the hanging drop vapor diffusion method
using dimethyl sulfoxide as the precipitating agent. The space group is P2(1)2(1)2(1). Unit cell dimensions are a = 44.1,
b = 57.1, and c = 61.7 A and alpha = beta = gamma = 90 degrees. The crystals diffract to beyond 1.7 A and are suitable for
high resolution data collection. Native diffraction data were collected. Screens for heavy atom derivatives have been initiated.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>PMID: 2784440</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Chromatography, Agarose ; Chromatography, DEAE-Cellulose ; Chromatography, Gel ; Electrophoresis, Polyacrylamide Gel ; Gas Chromatography-Mass Spectrometry ; Humans ; Interleukin-1 - isolation & purification ; Isoelectric Focusing ; man ; Molecular Sequence Data ; Recombinant Proteins - isolation & purification ; X-Ray Diffraction</subject><ispartof>The Journal of biological chemistry, 1989-03, Vol.264 (9), p.4948-4952</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2784440$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hassell, A M</creatorcontrib><creatorcontrib>Johanson, K O</creatorcontrib><creatorcontrib>Goodhart, P</creatorcontrib><creatorcontrib>Young, P R</creatorcontrib><creatorcontrib>Holskin, B P</creatorcontrib><creatorcontrib>Carr, S A</creatorcontrib><creatorcontrib>Roberts, G D</creatorcontrib><creatorcontrib>Simon, P L</creatorcontrib><creatorcontrib>Chen, M J</creatorcontrib><creatorcontrib>Lewis, M</creatorcontrib><title>Preliminary X-ray crystallography studies of recombinant human interleukin-1 alpha. Purification and structural characterization</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Human interleukin-1 alpha, cloned and expressed in E. coli, has been purified and structurally characterized by various physiochemical
methods, including mass spectrometry. The recombinant protein has been crystallized by the hanging drop vapor diffusion method
using dimethyl sulfoxide as the precipitating agent. The space group is P2(1)2(1)2(1). Unit cell dimensions are a = 44.1,
b = 57.1, and c = 61.7 A and alpha = beta = gamma = 90 degrees. The crystals diffract to beyond 1.7 A and are suitable for
high resolution data collection. Native diffraction data were collected. Screens for heavy atom derivatives have been initiated.</description><subject>Amino Acid Sequence</subject><subject>Chromatography, Agarose</subject><subject>Chromatography, DEAE-Cellulose</subject><subject>Chromatography, Gel</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Gas Chromatography-Mass Spectrometry</subject><subject>Humans</subject><subject>Interleukin-1 - isolation & purification</subject><subject>Isoelectric Focusing</subject><subject>man</subject><subject>Molecular Sequence Data</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>X-Ray Diffraction</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE9LxDAUxIso67r6EYTgwVslSdNucpTFf7DgHhT2VtL0ZRtN0zVpkHryoxt0777LO8xvBmaOsjnBvMiLkmyPsznGlOSClvw0OwvhDadjgsyyGV1yxhieZ98bD9b0xkk_oW3u5YSUn8IorR12Xu67CYUxtgYCGjTyoIa-SbAbURd76ZBxI3gL8d24nCBp9528QZvojTZKjmZwSLo2RfioxuilRaqTXqpkMl-_-nl2oqUNcHH4i-z1_u5l9Zivnx-eVrfrvKMVG_NGcEyVYryogJBKNC0uGibLVEdxJdsCGqYJh4oVWFOmdUHbtgSGOW6AaCgW2fVf7t4PHxHCWPcmKLBWOhhiqJdcYM6x-BckJeWM0jKBlwcwNj209d6bPq1YH7ZN-tWf3pld92k81I0ZVAd9nRrVomYitfkBXCiFWQ</recordid><startdate>19890325</startdate><enddate>19890325</enddate><creator>Hassell, A M</creator><creator>Johanson, K O</creator><creator>Goodhart, P</creator><creator>Young, P R</creator><creator>Holskin, B P</creator><creator>Carr, S A</creator><creator>Roberts, G D</creator><creator>Simon, P L</creator><creator>Chen, M J</creator><creator>Lewis, M</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19890325</creationdate><title>Preliminary X-ray crystallography studies of recombinant human interleukin-1 alpha. Purification and structural characterization</title><author>Hassell, A M ; Johanson, K O ; Goodhart, P ; Young, P R ; Holskin, B P ; Carr, S A ; Roberts, G D ; Simon, P L ; Chen, M J ; Lewis, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h264t-b9802cc4836e1169bd03b4a5491c8cad3eb4f18e6430f24ff32dd5e4080be1fe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Amino Acid Sequence</topic><topic>Chromatography, Agarose</topic><topic>Chromatography, DEAE-Cellulose</topic><topic>Chromatography, Gel</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Gas Chromatography-Mass Spectrometry</topic><topic>Humans</topic><topic>Interleukin-1 - isolation & purification</topic><topic>Isoelectric Focusing</topic><topic>man</topic><topic>Molecular Sequence Data</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>X-Ray Diffraction</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hassell, A M</creatorcontrib><creatorcontrib>Johanson, K O</creatorcontrib><creatorcontrib>Goodhart, P</creatorcontrib><creatorcontrib>Young, P R</creatorcontrib><creatorcontrib>Holskin, B P</creatorcontrib><creatorcontrib>Carr, S A</creatorcontrib><creatorcontrib>Roberts, G D</creatorcontrib><creatorcontrib>Simon, P L</creatorcontrib><creatorcontrib>Chen, M J</creatorcontrib><creatorcontrib>Lewis, M</creatorcontrib><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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hassell, A M</au><au>Johanson, K O</au><au>Goodhart, P</au><au>Young, P R</au><au>Holskin, B P</au><au>Carr, S A</au><au>Roberts, G D</au><au>Simon, P L</au><au>Chen, M J</au><au>Lewis, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Preliminary X-ray crystallography studies of recombinant human interleukin-1 alpha. Purification and structural characterization</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1989-03-25</date><risdate>1989</risdate><volume>264</volume><issue>9</issue><spage>4948</spage><epage>4952</epage><pages>4948-4952</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Human interleukin-1 alpha, cloned and expressed in E. coli, has been purified and structurally characterized by various physiochemical
methods, including mass spectrometry. The recombinant protein has been crystallized by the hanging drop vapor diffusion method
using dimethyl sulfoxide as the precipitating agent. The space group is P2(1)2(1)2(1). Unit cell dimensions are a = 44.1,
b = 57.1, and c = 61.7 A and alpha = beta = gamma = 90 degrees. The crystals diffract to beyond 1.7 A and are suitable for
high resolution data collection. Native diffraction data were collected. Screens for heavy atom derivatives have been initiated.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>2784440</pmid><tpages>5</tpages></addata></record> |
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| language | eng |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Chromatography, Agarose Chromatography, DEAE-Cellulose Chromatography, Gel Electrophoresis, Polyacrylamide Gel Gas Chromatography-Mass Spectrometry Humans Interleukin-1 - isolation & purification Isoelectric Focusing man Molecular Sequence Data Recombinant Proteins - isolation & purification X-Ray Diffraction |
| title | Preliminary X-ray crystallography studies of recombinant human interleukin-1 alpha. Purification and structural characterization |
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