Crystallization and preliminary X-ray analysis of the acyl carrier protein synthase (AcpS) from Staphylococcus aureus
Acyl carrier protein synthase (AcpS) catalyzes the transfer of 4′‐phophopantetheine from coenzyme A to the acyl carrier protein (ACP) to activate it for fatty‐acid biosynthesis. Two crystal forms of Staphylococcus aureus AcpS have been generated at 277 K using either NaCl or PEG 6000 as a precipita...
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| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2004-04, Vol.60 (4), p.773-774 |
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| container_title | Acta crystallographica. Section D, Biological crystallography. |
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| creator | Daubaras, Dayna L. Wilson, Eileen M. Black, Todd Strickland, Corey Beyer, Brian M. Orth, Peter |
| description | Acyl carrier protein synthase (AcpS) catalyzes the transfer of 4′‐phophopantetheine from coenzyme A to the acyl carrier protein (ACP) to activate it for fatty‐acid biosynthesis. Two crystal forms of Staphylococcus aureus AcpS have been generated at 277 K using either NaCl or PEG 6000 as a precipitant. The diffraction patterns of the crystals extend to 1.65 and 1.8 Å, respectively. Full sets of X‐ray diffraction data were collected from native crystals and the crystal structures were solved by molecular replacement. |
| doi_str_mv | 10.1107/S0907444904003282 |
| format | Article |
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Two crystal forms of Staphylococcus aureus AcpS have been generated at 277 K using either NaCl or PEG 6000 as a precipitant. The diffraction patterns of the crystals extend to 1.65 and 1.8 Å, respectively. Full sets of X‐ray diffraction data were collected from native crystals and the crystal structures were solved by molecular replacement.</description><identifier>ISSN: 1399-0047</identifier><identifier>ISSN: 0907-4449</identifier><identifier>EISSN: 1399-0047</identifier><identifier>DOI: 10.1107/S0907444904003282</identifier><identifier>PMID: 15039582</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>acyl carrier protein synthase ; Bacterial Proteins - chemistry ; Cloning, Molecular ; Crystallization ; Crystallography, X-Ray ; Polyethylene Glycols ; Sodium Chloride ; Solvents ; Staphylococcus aureus - enzymology ; Transferases (Other Substituted Phosphate Groups) - chemistry</subject><ispartof>Acta crystallographica. 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Full sets of X‐ray diffraction data were collected from native crystals and the crystal structures were solved by molecular replacement.</description><subject>acyl carrier protein synthase</subject><subject>Bacterial Proteins - chemistry</subject><subject>Cloning, Molecular</subject><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Polyethylene Glycols</subject><subject>Sodium Chloride</subject><subject>Solvents</subject><subject>Staphylococcus aureus - enzymology</subject><subject>Transferases (Other Substituted Phosphate Groups) - chemistry</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEuP0zAURi0EYh7wA9ggrxAsAtePxMmy6tCCNIJFQQxsLMe5Vg1O0rETQebXY9QKkFiw8kPnfLr3I-QJg5eMgXq1gwaUlLIBCSB4ze-RcyaapgCQ6v5f9zNykdJXAOBcqIfkjJUgmrLm52RexyVNJgR_ZyY_DtQMHT1EDL73g4kLvSmiWfKvCUvyiY6OTnukxi6BWhOjx5jxcUI_0LQM094kpM9X9rB7QV0ce7qbzGG_hNGO1s6JmjninB6RB86EhI9P5yX5uHn9Yf2muH6_fbteXRdWiBqKrpK1VIhNZVBUJTaucrLOL85YW8uWWeBW8rKTFptOIBeuFTwvXZWudUyJS_LsmJtHvJ0xTbr3yWIIZsBxTloxVTLOygyyI2jjmFJEpw_R93l_zUD_6lr_03V2np7C57bH7o9xKjcD9RH47gMu_0_Uq89X25sSGGS1OKo-Tfjjt2riN10poUr96d1WS1Z92VzJjWbiJxcymc8</recordid><startdate>200404</startdate><enddate>200404</enddate><creator>Daubaras, Dayna L.</creator><creator>Wilson, Eileen M.</creator><creator>Black, Todd</creator><creator>Strickland, Corey</creator><creator>Beyer, Brian M.</creator><creator>Orth, Peter</creator><general>International Union of Crystallography</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>200404</creationdate><title>Crystallization and preliminary X-ray analysis of the acyl carrier protein synthase (AcpS) from Staphylococcus aureus</title><author>Daubaras, Dayna L. ; Wilson, Eileen M. ; Black, Todd ; Strickland, Corey ; Beyer, Brian M. ; Orth, Peter</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3380-d64847ee96ae365e9f6f4896a211b84b1c02c425d4ce9d3e23fb3239965fbf173</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>acyl carrier protein synthase</topic><topic>Bacterial Proteins - chemistry</topic><topic>Cloning, Molecular</topic><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>Polyethylene Glycols</topic><topic>Sodium Chloride</topic><topic>Solvents</topic><topic>Staphylococcus aureus - enzymology</topic><topic>Transferases (Other Substituted Phosphate Groups) - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Daubaras, Dayna L.</creatorcontrib><creatorcontrib>Wilson, Eileen M.</creatorcontrib><creatorcontrib>Black, Todd</creatorcontrib><creatorcontrib>Strickland, Corey</creatorcontrib><creatorcontrib>Beyer, Brian M.</creatorcontrib><creatorcontrib>Orth, Peter</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. 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D</addtitle><date>2004-04</date><risdate>2004</risdate><volume>60</volume><issue>4</issue><spage>773</spage><epage>774</epage><pages>773-774</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>Acyl carrier protein synthase (AcpS) catalyzes the transfer of 4′‐phophopantetheine from coenzyme A to the acyl carrier protein (ACP) to activate it for fatty‐acid biosynthesis. Two crystal forms of Staphylococcus aureus AcpS have been generated at 277 K using either NaCl or PEG 6000 as a precipitant. The diffraction patterns of the crystals extend to 1.65 and 1.8 Å, respectively. Full sets of X‐ray diffraction data were collected from native crystals and the crystal structures were solved by molecular replacement.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>15039582</pmid><doi>10.1107/S0907444904003282</doi><tpages>2</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1399-0047 |
| ispartof | Acta crystallographica. Section D, Biological crystallography., 2004-04, Vol.60 (4), p.773-774 |
| issn | 1399-0047 0907-4449 1399-0047 |
| language | eng |
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| source | MEDLINE; Access via Wiley Online Library; Alma/SFX Local Collection |
| subjects | acyl carrier protein synthase Bacterial Proteins - chemistry Cloning, Molecular Crystallization Crystallography, X-Ray Polyethylene Glycols Sodium Chloride Solvents Staphylococcus aureus - enzymology Transferases (Other Substituted Phosphate Groups) - chemistry |
| title | Crystallization and preliminary X-ray analysis of the acyl carrier protein synthase (AcpS) from Staphylococcus aureus |
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