Multiple isomorphous replacement on merohedral twins: structure determination of deacetoxycephalosporin C synthase
Merohedral twinning is a packing anomaly that seriously impairs the determination of macromolecular crystal structures. Crystals of deacetoxycephalosporin C synthase (DAOCS), an enzyme involved in the expansion of the penicillin nucleus to form the core structure of the cephalosporin antibiotics, w...
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Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-12, Vol.57 (12), p.1776-1785 |
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container_title | Acta crystallographica. Section D, Biological crystallography. |
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creator | Terwisscha van Scheltinga, Anke C. Valegård, Karin Ramaswamy, S. Hajdu, Janos Andersson, Inger |
description | Merohedral twinning is a packing anomaly that seriously impairs the determination of macromolecular crystal structures. Crystals of deacetoxycephalosporin C synthase (DAOCS), an enzyme involved in the expansion of the penicillin nucleus to form the core structure of the cephalosporin antibiotics, were found to be merohedrally twinned by many diagnostic criteria. Here, the structure determination of DAOCS from twinned crystals based on a combination of isomorphous replacement and the use of a multiple‐wavelength diffraction data set is described. |
doi_str_mv | 10.1107/S0907444901014081 |
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Crystals of deacetoxycephalosporin C synthase (DAOCS), an enzyme involved in the expansion of the penicillin nucleus to form the core structure of the cephalosporin antibiotics, were found to be merohedrally twinned by many diagnostic criteria. Here, the structure determination of DAOCS from twinned crystals based on a combination of isomorphous replacement and the use of a multiple‐wavelength diffraction data set is described.</description><identifier>ISSN: 1399-0047</identifier><identifier>ISSN: 0907-4449</identifier><identifier>EISSN: 1399-0047</identifier><identifier>DOI: 10.1107/S0907444901014081</identifier><identifier>PMID: 11717489</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: Munksgaard International Publishers</publisher><subject>Crystallization ; Crystallography, X-Ray ; deacetoxycephalosporin C ; Intramolecular Transferases - chemistry ; merohedral twinning ; Models, Molecular ; Penicillin-Binding Proteins ; Protein Conformation</subject><ispartof>Acta crystallographica. 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Section D, Biological crystallography.</title><addtitle>Acta Cryst. D</addtitle><description>Merohedral twinning is a packing anomaly that seriously impairs the determination of macromolecular crystal structures. Crystals of deacetoxycephalosporin C synthase (DAOCS), an enzyme involved in the expansion of the penicillin nucleus to form the core structure of the cephalosporin antibiotics, were found to be merohedrally twinned by many diagnostic criteria. Here, the structure determination of DAOCS from twinned crystals based on a combination of isomorphous replacement and the use of a multiple‐wavelength diffraction data set is described.</description><subject>Crystallization</subject><subject>Crystallography, X-Ray</subject><subject>deacetoxycephalosporin C</subject><subject>Intramolecular Transferases - chemistry</subject><subject>merohedral twinning</subject><subject>Models, Molecular</subject><subject>Penicillin-Binding Proteins</subject><subject>Protein Conformation</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>eNqFkE2P0zAQhi0EYj_gB3BBPnELeGwntrmtutAFFhAUhDhZrjNRDUkcbEe7_fcEtQIkDpw8sp7n1cxLyCNgTwGYerZhhikppWHAQDINd8gpCGMqxqS6-9d8Qs5y_sYY41yo--QEQIGS2pyS9HbuS5h6pCHHIaZpF-dME0698zjgWGgc6YAp7rBNrqflJoz5Oc0lzb7MCWmLBdMQRlfCQsZu-VjMEm_3Hqed62OeYgojXdG8H8vOZXxA7nWuz_jw-J6Tzy9ffFpdVdfv169WF9eVF1rWlQC1FW1X153gzjVYm62WjeLeu2VzYbiuPbQaDHRaIzTgOQrFOMq2Vrph4pw8OeROKf6YMRc7hOyx792Iy5FWcW4kGLOAcAB9ijkn7OyUwuDS3gKzv4q2_xS9OI-P4fN2wPaPcWx2AfQBuAk97v-faC--Xq4_chD1olYHNeSCt79Vl77bRglV2y_v1vZ18-bDhm3AGvETy0WZ2A</recordid><startdate>200112</startdate><enddate>200112</enddate><creator>Terwisscha van Scheltinga, Anke C.</creator><creator>Valegård, Karin</creator><creator>Ramaswamy, S.</creator><creator>Hajdu, Janos</creator><creator>Andersson, Inger</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>200112</creationdate><title>Multiple isomorphous replacement on merohedral twins: structure determination of deacetoxycephalosporin C synthase</title><author>Terwisscha van Scheltinga, Anke C. ; Valegård, Karin ; Ramaswamy, S. ; Hajdu, Janos ; Andersson, Inger</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3845-317b3df55f32aa6e59b84672cca48939285c1d8191f88e161c2e3702e4d578603</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Crystallization</topic><topic>Crystallography, X-Ray</topic><topic>deacetoxycephalosporin C</topic><topic>Intramolecular Transferases - chemistry</topic><topic>merohedral twinning</topic><topic>Models, Molecular</topic><topic>Penicillin-Binding Proteins</topic><topic>Protein Conformation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Terwisscha van Scheltinga, Anke C.</creatorcontrib><creatorcontrib>Valegård, Karin</creatorcontrib><creatorcontrib>Ramaswamy, S.</creatorcontrib><creatorcontrib>Hajdu, Janos</creatorcontrib><creatorcontrib>Andersson, Inger</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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Crystals of deacetoxycephalosporin C synthase (DAOCS), an enzyme involved in the expansion of the penicillin nucleus to form the core structure of the cephalosporin antibiotics, were found to be merohedrally twinned by many diagnostic criteria. Here, the structure determination of DAOCS from twinned crystals based on a combination of isomorphous replacement and the use of a multiple‐wavelength diffraction data set is described.</abstract><cop>5 Abbey Square, Chester, Cheshire CH1 2HU, England</cop><pub>Munksgaard International Publishers</pub><pmid>11717489</pmid><doi>10.1107/S0907444901014081</doi><tpages>10</tpages></addata></record> |
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source | MEDLINE; Crystallography Journals Online; Wiley Online Library Journals Frontfile Complete; Alma/SFX Local Collection |
subjects | Crystallization Crystallography, X-Ray deacetoxycephalosporin C Intramolecular Transferases - chemistry merohedral twinning Models, Molecular Penicillin-Binding Proteins Protein Conformation |
title | Multiple isomorphous replacement on merohedral twins: structure determination of deacetoxycephalosporin C synthase |
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