Crystallographic studies and preliminary X-ray investigation of (S)-p-hydroxy-mandelonitrile lyase from Sorghum bicolor (L.)
(S)‐p‐Hydroxy‐mandelonitrile lyase from Sorghum bicolor has been crystallized in three different forms using the hanging‐drop vapor‐diffusion technique. Crystal form I is obtained from 1.4 M (NH4)2SO4 in 100 mM Na‐acetate, pH 4.6, and belongs to the orthorhombic space group P212121. The cell dimensi...
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Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1996-07, Vol.52 (4), p.887-889 |
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container_title | Acta crystallographica. Section D, Biological crystallography. |
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creator | Lauble, H. Knödler, S. Schindelin, H. Förster, S. Wajant, H. Effenberger, F. |
description | (S)‐p‐Hydroxy‐mandelonitrile lyase from Sorghum bicolor has been crystallized in three different forms using the hanging‐drop vapor‐diffusion technique. Crystal form I is obtained from 1.4 M (NH4)2SO4 in 100 mM Na‐acetate, pH 4.6, and belongs to the orthorhombic space group P212121. The cell dimensions are a = 71.4, b = 95.8, c = 149.1 Å. A complete set of diffraction data has been collected to 2.6 Å resolution. Form II crystals are grown from 500 mM Li2SO4 in 13% polyethylene glycol 8000. These crystals appear as hexagonal plates and diffract to 2.98 Å resolution but apparently are twinned. Cocrystallizing hydroxynitrile lyase with the inhibitor benzoic acid using 1.4 M (NH4)2SO4 in 100 mM Na citrate, pH 5.4 as precipitant yields crystal form III, which belongs to the monoclinic space group C2 with a = 150.7, b = 103.7, c = 90.6 Å, β = 101.3. X‐ray diffraction data were collected to 2.3 Å resolution. |
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Crystal form I is obtained from 1.4 M (NH4)2SO4 in 100 mM Na‐acetate, pH 4.6, and belongs to the orthorhombic space group P212121. The cell dimensions are a = 71.4, b = 95.8, c = 149.1 Å. A complete set of diffraction data has been collected to 2.6 Å resolution. Form II crystals are grown from 500 mM Li2SO4 in 13% polyethylene glycol 8000. These crystals appear as hexagonal plates and diffract to 2.98 Å resolution but apparently are twinned. Cocrystallizing hydroxynitrile lyase with the inhibitor benzoic acid using 1.4 M (NH4)2SO4 in 100 mM Na citrate, pH 5.4 as precipitant yields crystal form III, which belongs to the monoclinic space group C2 with a = 150.7, b = 103.7, c = 90.6 Å, β = 101.3. X‐ray diffraction data were collected to 2.3 Å resolution.</description><identifier>ISSN: 1399-0047</identifier><identifier>ISSN: 0907-4449</identifier><identifier>EISSN: 1399-0047</identifier><identifier>DOI: 10.1107/S0907444996002399</identifier><identifier>PMID: 15299660</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><ispartof>Acta crystallographica. 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Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>(S)‐p‐Hydroxy‐mandelonitrile lyase from Sorghum bicolor has been crystallized in three different forms using the hanging‐drop vapor‐diffusion technique. Crystal form I is obtained from 1.4 M (NH4)2SO4 in 100 mM Na‐acetate, pH 4.6, and belongs to the orthorhombic space group P212121. The cell dimensions are a = 71.4, b = 95.8, c = 149.1 Å. A complete set of diffraction data has been collected to 2.6 Å resolution. Form II crystals are grown from 500 mM Li2SO4 in 13% polyethylene glycol 8000. These crystals appear as hexagonal plates and diffract to 2.98 Å resolution but apparently are twinned. Cocrystallizing hydroxynitrile lyase with the inhibitor benzoic acid using 1.4 M (NH4)2SO4 in 100 mM Na citrate, pH 5.4 as precipitant yields crystal form III, which belongs to the monoclinic space group C2 with a = 150.7, b = 103.7, c = 90.6 Å, β = 101.3. X‐ray diffraction data were collected to 2.3 Å resolution.</description><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNqFkM1u1DAUhSMEoqXwAGyQV6hduNixHY-X1bS0SCNYpPxuLMc_MwYnDnYCjcTDYzQjQGLB6t7F-Y7u_arqKUbnGCP-okUCcUqpEA1CNRHiXnWMy4AIUX7_r_2oepTzZ1RCNeEPqyPM6sI06Lj6sU5LnlQIcZvUuPMa5Gk23magBgPGZIPv_aDSAj7ApBbgh282T36rJh8HEB04bc_gCHeLSfFugX2hbIiDn5IPFoRFZQtcij1oY9ru5h50XscQEzjdnJ89rh44FbJ9cpgn1duXV7frG7h5c_1qfbGBmnKBIeMNYQyxVcOU1kIYrJ2hqNFN5wwuDhTRjakN7SwzTmBmiaa1Va5mHTXOkpPq-b53TPHrXO6Xvc_ahqAGG-csORc1J2JVgngf1CnmnKyTY_J9-V5iJH8pl_8oL8yzQ_nc9db8IQ6OS2C1D3wvSpb_N8qLj5ftFcICFxTuUZ8ne_cbVemLbDjhTL5_fS3f3X6qCWpv5CX5Ca0CnWY</recordid><startdate>199607</startdate><enddate>199607</enddate><creator>Lauble, H.</creator><creator>Knödler, S.</creator><creator>Schindelin, H.</creator><creator>Förster, S.</creator><creator>Wajant, H.</creator><creator>Effenberger, F.</creator><general>International Union of Crystallography</general><scope>BSCLL</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>199607</creationdate><title>Crystallographic studies and preliminary X-ray investigation of (S)-p-hydroxy-mandelonitrile lyase from Sorghum bicolor (L.)</title><author>Lauble, H. ; Knödler, S. ; Schindelin, H. ; Förster, S. ; Wajant, H. ; Effenberger, F.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4791-57635505865acc99d1cfd406c6bfd1090a3c6d2d4be5df915e3c42eaf25b4dfe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lauble, H.</creatorcontrib><creatorcontrib>Knödler, S.</creatorcontrib><creatorcontrib>Schindelin, H.</creatorcontrib><creatorcontrib>Förster, S.</creatorcontrib><creatorcontrib>Wajant, H.</creatorcontrib><creatorcontrib>Effenberger, F.</creatorcontrib><collection>Istex</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>Lauble, H.</au><au>Knödler, S.</au><au>Schindelin, H.</au><au>Förster, S.</au><au>Wajant, H.</au><au>Effenberger, F.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallographic studies and preliminary X-ray investigation of (S)-p-hydroxy-mandelonitrile lyase from Sorghum bicolor (L.)</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><addtitle>Acta Cryst. D</addtitle><date>1996-07</date><risdate>1996</risdate><volume>52</volume><issue>4</issue><spage>887</spage><epage>889</epage><pages>887-889</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>(S)‐p‐Hydroxy‐mandelonitrile lyase from Sorghum bicolor has been crystallized in three different forms using the hanging‐drop vapor‐diffusion technique. Crystal form I is obtained from 1.4 M (NH4)2SO4 in 100 mM Na‐acetate, pH 4.6, and belongs to the orthorhombic space group P212121. The cell dimensions are a = 71.4, b = 95.8, c = 149.1 Å. A complete set of diffraction data has been collected to 2.6 Å resolution. Form II crystals are grown from 500 mM Li2SO4 in 13% polyethylene glycol 8000. These crystals appear as hexagonal plates and diffract to 2.98 Å resolution but apparently are twinned. Cocrystallizing hydroxynitrile lyase with the inhibitor benzoic acid using 1.4 M (NH4)2SO4 in 100 mM Na citrate, pH 5.4 as precipitant yields crystal form III, which belongs to the monoclinic space group C2 with a = 150.7, b = 103.7, c = 90.6 Å, β = 101.3. X‐ray diffraction data were collected to 2.3 Å resolution.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>International Union of Crystallography</pub><pmid>15299660</pmid><doi>10.1107/S0907444996002399</doi><tpages>3</tpages></addata></record> |
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title | Crystallographic studies and preliminary X-ray investigation of (S)-p-hydroxy-mandelonitrile lyase from Sorghum bicolor (L.) |
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