Characterization and crystallization of a novel Sarcocystis muris lectin, SML-2
A novel lectin (SML‐2) consisting of 138 amino acids was isolated from cyst merozoites of Sarcocystis muris and sequenced by Edman degradation and mass spectrometry. All 12 cysteinyl residues are involved in disulfide bridges, four of which are attributed to a characteristic pattern of cysteines as...
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| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-07, Vol.57 (7), p.1042-1045 |
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| container_title | Acta crystallographica. Section D, Biological crystallography. |
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| creator | Müller, Jürgen J. Müller, Eva-Christina Montag, Thomas Zyto, Nadja Löschner, Bettina Klein, Harald Heineman, Udo Otto, Albrecht |
| description | A novel lectin (SML‐2) consisting of 138 amino acids was isolated from cyst merozoites of Sarcocystis muris and sequenced by Edman degradation and mass spectrometry. All 12 cysteinyl residues are involved in disulfide bridges, four of which are attributed to a characteristic pattern of cysteines as found in the so‐called PAN‐module superfamily. Crystals of SML‐2 diffracting to 2.1 Å resolution at a synchrotron were grown by the hanging‐drop vapour‐diffusion technique. They belong to the space group P212121, with unit‐cell parameters a = 53.6, b = 128.8, c = 158.2 Å and eight molecules in the asymmetric unit. SML‐2 cocrystallized with Au galactose results in two different crystal forms. The first form is isomorphous with the native crystals and the second form adopts space group C2221, with unit‐cell parameters a = 74.7, b = 82.0, c = 131.0 Å, and diffracts to 2.4 Å at a rotating‐anode X‐ray generator. |
| doi_str_mv | 10.1107/S0907444901007284 |
| format | Article |
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All 12 cysteinyl residues are involved in disulfide bridges, four of which are attributed to a characteristic pattern of cysteines as found in the so‐called PAN‐module superfamily. Crystals of SML‐2 diffracting to 2.1 Å resolution at a synchrotron were grown by the hanging‐drop vapour‐diffusion technique. They belong to the space group P212121, with unit‐cell parameters a = 53.6, b = 128.8, c = 158.2 Å and eight molecules in the asymmetric unit. SML‐2 cocrystallized with Au galactose results in two different crystal forms. The first form is isomorphous with the native crystals and the second form adopts space group C2221, with unit‐cell parameters a = 74.7, b = 82.0, c = 131.0 Å, and diffracts to 2.4 Å at a rotating‐anode X‐ray generator.</description><identifier>ISSN: 1399-0047</identifier><identifier>ISSN: 0907-4449</identifier><identifier>EISSN: 1399-0047</identifier><identifier>DOI: 10.1107/S0907444901007284</identifier><identifier>PMID: 11418777</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers</publisher><subject>Amino Acid Sequence ; Animals ; Crystallization ; Crystallography, X-Ray ; lectins ; Lectins - chemistry ; Molecular Sequence Data ; Sarcocystis - chemistry ; Sarcocystis muris ; Sequence Homology, Amino Acid ; Spectrometry, Mass, Electrospray Ionization</subject><ispartof>Acta crystallographica. Section D, Biological crystallography., 2001-07, Vol.57 (7), p.1042-1045</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c3845-d0cfb08d04cd28f38ab46bb8ae0c4b3b38ad03ef8d32e1929fa5bbe59ee51ae93</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1107%2FS0907444901007284$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1107%2FS0907444901007284$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,3987,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11418777$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Müller, Jürgen J.</creatorcontrib><creatorcontrib>Müller, Eva-Christina</creatorcontrib><creatorcontrib>Montag, Thomas</creatorcontrib><creatorcontrib>Zyto, Nadja</creatorcontrib><creatorcontrib>Löschner, Bettina</creatorcontrib><creatorcontrib>Klein, Harald</creatorcontrib><creatorcontrib>Heineman, Udo</creatorcontrib><creatorcontrib>Otto, Albrecht</creatorcontrib><title>Characterization and crystallization of a novel Sarcocystis muris lectin, SML-2</title><title>Acta crystallographica. Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>A novel lectin (SML‐2) consisting of 138 amino acids was isolated from cyst merozoites of Sarcocystis muris and sequenced by Edman degradation and mass spectrometry. All 12 cysteinyl residues are involved in disulfide bridges, four of which are attributed to a characteristic pattern of cysteines as found in the so‐called PAN‐module superfamily. Crystals of SML‐2 diffracting to 2.1 Å resolution at a synchrotron were grown by the hanging‐drop vapour‐diffusion technique. They belong to the space group P212121, with unit‐cell parameters a = 53.6, b = 128.8, c = 158.2 Å and eight molecules in the asymmetric unit. SML‐2 cocrystallized with Au galactose results in two different crystal forms. The first form is isomorphous with the native crystals and the second form adopts space group C2221, with unit‐cell parameters a = 74.7, b = 82.0, c = 131.0 Å, and diffracts to 2.4 Å at a rotating‐anode X‐ray generator.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>lectins</subject><subject>Lectins - chemistry</subject><subject>Molecular Sequence Data</subject><subject>Sarcocystis - chemistry</subject><subject>Sarcocystis muris</subject><subject>Sequence Homology, Amino Acid</subject><subject>Spectrometry, Mass, Electrospray Ionization</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtPwzAQhC0E4v0DuKCcOBFYxw62j6XlJRWKVKqKk2U7GxFIk2KnQPn1BLU8JA5cdlez881hCNmjcEQpiOMhKBCccwUUQCSSr5BNypSKAbhY_XVvkK0QHgEgSZhYJxuUciqFEJtk0H0w3rgGffFumqKuIlNlkfPz0Jiy_NLqPDJRVb9gGQ2Nd7Vr30WIJjPfzhJdU1SH0fC6Hyc7ZC03ZcDd5d4mo_Ozu-5l3B9cXHU7_dgxydM4A5dbkBlwlyUyZ9JYfmKtNAiOW2ZbIQOGucxYglQlKjeptZgqxJQaVGybHCxyp75-nmFo9KQIDsvSVFjPghagmGCUt0a6MDpfh-Ax11NfTIyfawr6s0X9p8WW2V-Gz-wEsx9iWVtrkAvDa1Hi_P9E3bnv3Y7a_tMWjRdoERp8-0aNf9IngolUj28u9E1v3FdcnGrBPgDBF4zP</recordid><startdate>200107</startdate><enddate>200107</enddate><creator>Müller, Jürgen J.</creator><creator>Müller, Eva-Christina</creator><creator>Montag, Thomas</creator><creator>Zyto, Nadja</creator><creator>Löschner, Bettina</creator><creator>Klein, Harald</creator><creator>Heineman, Udo</creator><creator>Otto, Albrecht</creator><general>Munksgaard International Publishers</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>200107</creationdate><title>Characterization and crystallization of a novel Sarcocystis muris lectin, SML-2</title><author>Müller, Jürgen J. ; Müller, Eva-Christina ; Montag, Thomas ; Zyto, Nadja ; Löschner, Bettina ; Klein, Harald ; Heineman, Udo ; Otto, Albrecht</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3845-d0cfb08d04cd28f38ab46bb8ae0c4b3b38ad03ef8d32e1929fa5bbe59ee51ae93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>lectins</topic><topic>Lectins - chemistry</topic><topic>Molecular Sequence Data</topic><topic>Sarcocystis - chemistry</topic><topic>Sarcocystis muris</topic><topic>Sequence Homology, Amino Acid</topic><topic>Spectrometry, Mass, Electrospray Ionization</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Müller, Jürgen J.</creatorcontrib><creatorcontrib>Müller, Eva-Christina</creatorcontrib><creatorcontrib>Montag, Thomas</creatorcontrib><creatorcontrib>Zyto, Nadja</creatorcontrib><creatorcontrib>Löschner, Bettina</creatorcontrib><creatorcontrib>Klein, Harald</creatorcontrib><creatorcontrib>Heineman, Udo</creatorcontrib><creatorcontrib>Otto, Albrecht</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>Acta crystallographica. Section D, Biological crystallography.</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Müller, Jürgen J.</au><au>Müller, Eva-Christina</au><au>Montag, Thomas</au><au>Zyto, Nadja</au><au>Löschner, Bettina</au><au>Klein, Harald</au><au>Heineman, Udo</au><au>Otto, Albrecht</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization and crystallization of a novel Sarcocystis muris lectin, SML-2</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><addtitle>Acta Cryst. D</addtitle><date>2001-07</date><risdate>2001</risdate><volume>57</volume><issue>7</issue><spage>1042</spage><epage>1045</epage><pages>1042-1045</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>A novel lectin (SML‐2) consisting of 138 amino acids was isolated from cyst merozoites of Sarcocystis muris and sequenced by Edman degradation and mass spectrometry. All 12 cysteinyl residues are involved in disulfide bridges, four of which are attributed to a characteristic pattern of cysteines as found in the so‐called PAN‐module superfamily. Crystals of SML‐2 diffracting to 2.1 Å resolution at a synchrotron were grown by the hanging‐drop vapour‐diffusion technique. They belong to the space group P212121, with unit‐cell parameters a = 53.6, b = 128.8, c = 158.2 Å and eight molecules in the asymmetric unit. SML‐2 cocrystallized with Au galactose results in two different crystal forms. The first form is isomorphous with the native crystals and the second form adopts space group C2221, with unit‐cell parameters a = 74.7, b = 82.0, c = 131.0 Å, and diffracts to 2.4 Å at a rotating‐anode X‐ray generator.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>11418777</pmid><doi>10.1107/S0907444901007284</doi><tpages>4</tpages></addata></record> |
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| source | MEDLINE; Crystallography Journals Online; Access via Wiley Online Library; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Crystallization Crystallography, X-Ray lectins Lectins - chemistry Molecular Sequence Data Sarcocystis - chemistry Sarcocystis muris Sequence Homology, Amino Acid Spectrometry, Mass, Electrospray Ionization |
| title | Characterization and crystallization of a novel Sarcocystis muris lectin, SML-2 |
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