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Crystallization and preliminary X-ray characterization of a thermostable pectate lyase from Thermotoga maritima
Pectate lyase is an enzyme involved in the degradation of the pectate portion of the primary plant cell wall. A recombinant pectate lyase from Thermotoga maritima where three of the four cysteine residues have been mutated (C132I, C156N, C194L) has been crystallized. Crystals of the same morphology...
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Published in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2002-04, Vol.58 (4), p.709-711 |
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container_title | Acta crystallographica. Section D, Biological crystallography. |
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creator | McDonough, Michael A. Ryttersgaard, Carsten Bjørnvad, Mads Eskelund Lo Leggio, Leila Schülein, Martin Schrøder Glad, Sanne O. Larsen, Sine |
description | Pectate lyase is an enzyme involved in the degradation of the pectate portion of the primary plant cell wall. A recombinant pectate lyase from Thermotoga maritima where three of the four cysteine residues have been mutated (C132I, C156N, C194L) has been crystallized. Crystals of the same morphology and trigonal space group R3 with similar unit‐cell parameters were obtained under two different conditions. The first, 0.3 M (NH4)H2PO4 pH 4.2, gave crystals with a maximum size of 0.4 × 0.2 × 0.2 mm in one week that diffracted to a resolution of 1.87 Å and had unit‐cell parameters a = b = 80.6, c = 148.8 Å. The second, 0.1 M sodium acetate, 6%(w/v) PEG 4000 pH 6.5, gave the same size crystals in two weeks that diffracted to a resolution of 2.1 Å and had unit‐cell parameters a = b = 80.0, c = 150.1 Å. |
doi_str_mv | 10.1107/S0907444902003827 |
format | article |
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A recombinant pectate lyase from Thermotoga maritima where three of the four cysteine residues have been mutated (C132I, C156N, C194L) has been crystallized. Crystals of the same morphology and trigonal space group R3 with similar unit‐cell parameters were obtained under two different conditions. The first, 0.3 M (NH4)H2PO4 pH 4.2, gave crystals with a maximum size of 0.4 × 0.2 × 0.2 mm in one week that diffracted to a resolution of 1.87 Å and had unit‐cell parameters a = b = 80.6, c = 148.8 Å. The second, 0.1 M sodium acetate, 6%(w/v) PEG 4000 pH 6.5, gave the same size crystals in two weeks that diffracted to a resolution of 2.1 Å and had unit‐cell parameters a = b = 80.0, c = 150.1 Å.</description><identifier>ISSN: 1399-0047</identifier><identifier>ISSN: 0907-4449</identifier><identifier>EISSN: 1399-0047</identifier><identifier>DOI: 10.1107/S0907444902003827</identifier><identifier>PMID: 11914504</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers</publisher><subject>Crystallization ; Crystallography, X-Ray ; Enzyme Stability ; Heating ; Mutation ; pectate lyase ; Polysaccharide-Lyases - chemistry ; Polysaccharide-Lyases - genetics ; Thermotoga maritima - chemistry</subject><ispartof>Acta crystallographica. 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Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>Pectate lyase is an enzyme involved in the degradation of the pectate portion of the primary plant cell wall. A recombinant pectate lyase from Thermotoga maritima where three of the four cysteine residues have been mutated (C132I, C156N, C194L) has been crystallized. Crystals of the same morphology and trigonal space group R3 with similar unit‐cell parameters were obtained under two different conditions. The first, 0.3 M (NH4)H2PO4 pH 4.2, gave crystals with a maximum size of 0.4 × 0.2 × 0.2 mm in one week that diffracted to a resolution of 1.87 Å and had unit‐cell parameters a = b = 80.6, c = 148.8 Å. The second, 0.1 M sodium acetate, 6%(w/v) PEG 4000 pH 6.5, gave the same size crystals in two weeks that diffracted to a resolution of 2.1 Å and had unit‐cell parameters a = b = 80.0, c = 150.1 Å.</description><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>Enzyme Stability</subject><subject>Heating</subject><subject>Mutation</subject><subject>pectate lyase</subject><subject>Polysaccharide-Lyases - chemistry</subject><subject>Polysaccharide-Lyases - genetics</subject><subject>Thermotoga maritima - chemistry</subject><issn>1399-0047</issn><issn>0907-4449</issn><issn>1399-0047</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><recordid>eNqFkU1v1DAQhi0EoqXwA7ggn7iF2rEdx8fVQlvUqhxaBPRiTZwJNTjrxfaqDb--aXf5kDhw8kh-nlejdwh5ydkbzpk-vGCGaSmlYTVjoq31I7LPhTEVY1I__mveI89y_sYYq2uhn5I9zg2Xisl9EpdpygVC8D-h-LiisOrpOmHwo19BmujnKsFE3TUkcAXTLywOFGi5xjTGWe8C0jW6AgVpmCAjHVIc6eXDf4lfgY6QfPEjPCdPBggZX-zeA_Lx6N3l8qQ6-3D8frk4q5xoZVs1jRNG1sCN6w2gc8a1Wum-GyTjgJ0W2LbIjXK16Trdu65GznWjHMdesUYckNfb3HWKPzaYix19dhgCrDBustVcKS7EPci3oEsx54SDXad5zzRZzux9y_aflmfn1S58043Y_zF2tc5AuwVufMDp_4l28eXt1WK-VDur1Vb1ueDtbxXSd9tooZX9dH5sT68Uuzg_kvZE3AGmTJlE</recordid><startdate>200204</startdate><enddate>200204</enddate><creator>McDonough, Michael A.</creator><creator>Ryttersgaard, Carsten</creator><creator>Bjørnvad, Mads Eskelund</creator><creator>Lo Leggio, Leila</creator><creator>Schülein, Martin</creator><creator>Schrøder Glad, Sanne O.</creator><creator>Larsen, Sine</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>200204</creationdate><title>Crystallization and preliminary X-ray characterization of a thermostable pectate lyase from Thermotoga maritima</title><author>McDonough, Michael A. ; Ryttersgaard, Carsten ; Bjørnvad, Mads Eskelund ; Lo Leggio, Leila ; Schülein, Martin ; Schrøder Glad, Sanne O. ; Larsen, Sine</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3848-66c3942a19cd9aecc9c8757dbf401aeb73e88e195c29bb7dcb2e11765c1ed5063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>Enzyme Stability</topic><topic>Heating</topic><topic>Mutation</topic><topic>pectate lyase</topic><topic>Polysaccharide-Lyases - chemistry</topic><topic>Polysaccharide-Lyases - genetics</topic><topic>Thermotoga maritima - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McDonough, Michael A.</creatorcontrib><creatorcontrib>Ryttersgaard, Carsten</creatorcontrib><creatorcontrib>Bjørnvad, Mads Eskelund</creatorcontrib><creatorcontrib>Lo Leggio, Leila</creatorcontrib><creatorcontrib>Schülein, Martin</creatorcontrib><creatorcontrib>Schrøder Glad, Sanne O.</creatorcontrib><creatorcontrib>Larsen, Sine</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>McDonough, Michael A.</au><au>Ryttersgaard, Carsten</au><au>Bjørnvad, Mads Eskelund</au><au>Lo Leggio, Leila</au><au>Schülein, Martin</au><au>Schrøder Glad, Sanne O.</au><au>Larsen, Sine</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary X-ray characterization of a thermostable pectate lyase from Thermotoga maritima</atitle><jtitle>Acta crystallographica. Section D, Biological crystallography.</jtitle><addtitle>Acta Cryst. D</addtitle><date>2002-04</date><risdate>2002</risdate><volume>58</volume><issue>4</issue><spage>709</spage><epage>711</epage><pages>709-711</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>Pectate lyase is an enzyme involved in the degradation of the pectate portion of the primary plant cell wall. A recombinant pectate lyase from Thermotoga maritima where three of the four cysteine residues have been mutated (C132I, C156N, C194L) has been crystallized. Crystals of the same morphology and trigonal space group R3 with similar unit‐cell parameters were obtained under two different conditions. The first, 0.3 M (NH4)H2PO4 pH 4.2, gave crystals with a maximum size of 0.4 × 0.2 × 0.2 mm in one week that diffracted to a resolution of 1.87 Å and had unit‐cell parameters a = b = 80.6, c = 148.8 Å. The second, 0.1 M sodium acetate, 6%(w/v) PEG 4000 pH 6.5, gave the same size crystals in two weeks that diffracted to a resolution of 2.1 Å and had unit‐cell parameters a = b = 80.0, c = 150.1 Å.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>11914504</pmid><doi>10.1107/S0907444902003827</doi><tpages>3</tpages></addata></record> |
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subjects | Crystallization Crystallography, X-Ray Enzyme Stability Heating Mutation pectate lyase Polysaccharide-Lyases - chemistry Polysaccharide-Lyases - genetics Thermotoga maritima - chemistry |
title | Crystallization and preliminary X-ray characterization of a thermostable pectate lyase from Thermotoga maritima |
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