{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,31]],"date-time":"2026-03-31T16:16:51Z","timestamp":1774973811148,"version":"3.50.1"},"reference-count":33,"publisher":"Proceedings of the National Academy of Sciences","issue":"26","license":[{"start":{"date-parts":[[2016,6,13]],"date-time":"2016-06-13T00:00:00Z","timestamp":1465776000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/www.pnas.org\/preview_site\/misc\/userlicense.xhtml"}],"funder":[{"DOI":"10.13039\/501100000780","name":"European Commission","doi-asserted-by":"publisher","award":["263916"],"award-info":[{"award-number":["263916"]}],"id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2016,6,28]]},"abstract":"<jats:title>Significance<\/jats:title>\n          <jats:p>\n            Plant cell wall (PCW) polysaccharide degradation is an important biological and industrial process. Noncatalytic carbohydrate binding modules (CBMs) fulfill a critical targeting function in PCW depolymerization.\n            <jats:italic>Ruminococcus flavefaciens<\/jats:italic>\n            synthesizes a highly efficient PCW degrading apparatus. Here, six previously unidentified\n            <jats:italic>R. flavefaciens<\/jats:italic>\n            CBM families were identified that targeted \u03b2-glucans, \u03b2-mannans, and pectins. Crystal structures of these CBMs revealed that recognition of \u03b2-glucans and \u03b2-mannans was mediated by differences in the conformation of conserved aromatic residues in the ligand binding cleft. A cluster of basic residues in CBM77 confers calcium-independent recognition of homogalacturonan. This report shows that the expansion of protein modules in the cellulosome of\n            <jats:italic>R. flavefaciens<\/jats:italic>\n            contributes to an extended CBM profile that supports efficient PCW degradation.\n          <\/jats:p>","DOI":"10.1073\/pnas.1601558113","type":"journal-article","created":{"date-parts":[[2016,6,14]],"date-time":"2016-06-14T03:05:39Z","timestamp":1465873539000},"page":"7136-7141","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":71,"title":["Complexity of the\n            <i>Ruminococcus flavefaciens<\/i>\n            cellulosome reflects an expansion in glycan recognition"],"prefix":"10.1073","volume":"113","author":[{"given":"Immacolata","family":"Venditto","sequence":"first","affiliation":[{"name":"Interdisciplinary Centre of Research in Animal Health, Faculdade de Medicina Veterin\u00e1ria, Universidade de Lisboa, P\u00f3lo Universit\u00e1rio do Alto da Ajuda, 1300-477 Lisbon, Portugal;"},{"name":"Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom;"}]},{"given":"Ana S.","family":"Luis","sequence":"additional","affiliation":[{"name":"Interdisciplinary Centre of Research in Animal Health, Faculdade de Medicina Veterin\u00e1ria, Universidade de Lisboa, P\u00f3lo Universit\u00e1rio do Alto da Ajuda, 1300-477 Lisbon, Portugal;"},{"name":"Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom;"}]},{"given":"Maja","family":"Rydahl","sequence":"additional","affiliation":[{"name":"Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Copenhagen, Denmark;"}]},{"given":"Julia","family":"Sch\u00fcckel","sequence":"additional","affiliation":[{"name":"Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Copenhagen, Denmark;"}]},{"given":"V\u00e2nia O.","family":"Fernandes","sequence":"additional","affiliation":[{"name":"Interdisciplinary Centre of Research in Animal Health, Faculdade de Medicina Veterin\u00e1ria, Universidade de Lisboa, P\u00f3lo Universit\u00e1rio do Alto da Ajuda, 1300-477 Lisbon, Portugal;"},{"name":"NZYTech Genes &amp; Enzymes, Campus do Lumiar, 1649-038 Lisbon, Portugal;"}]},{"given":"Silvia","family":"Vidal-Melgosa","sequence":"additional","affiliation":[{"name":"Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Copenhagen, Denmark;"}]},{"given":"Pedro","family":"Bule","sequence":"additional","affiliation":[{"name":"Interdisciplinary Centre of Research in Animal Health, Faculdade de Medicina Veterin\u00e1ria, Universidade de Lisboa, P\u00f3lo Universit\u00e1rio do Alto da Ajuda, 1300-477 Lisbon, Portugal;"}]},{"given":"Arun","family":"Goyal","sequence":"additional","affiliation":[{"name":"Department of Biotechnology, Indian Institute of Technology Guwahati, Guwahati, Assam, India;"}]},{"given":"Virginia M. R.","family":"Pires","sequence":"additional","affiliation":[{"name":"Interdisciplinary Centre of Research in Animal Health, Faculdade de Medicina Veterin\u00e1ria, Universidade de Lisboa, P\u00f3lo Universit\u00e1rio do Alto da Ajuda, 1300-477 Lisbon, Portugal;"}]},{"given":"Catarina G.","family":"Dourado","sequence":"additional","affiliation":[{"name":"Interdisciplinary Centre of Research in Animal Health, Faculdade de Medicina Veterin\u00e1ria, Universidade de Lisboa, P\u00f3lo Universit\u00e1rio do Alto da Ajuda, 1300-477 Lisbon, Portugal;"}]},{"given":"Lu\u00eds M. A.","family":"Ferreira","sequence":"additional","affiliation":[{"name":"Interdisciplinary Centre of Research in Animal Health, Faculdade de Medicina Veterin\u00e1ria, Universidade de Lisboa, P\u00f3lo Universit\u00e1rio do Alto da Ajuda, 1300-477 Lisbon, Portugal;"},{"name":"NZYTech Genes &amp; Enzymes, Campus do Lumiar, 1649-038 Lisbon, Portugal;"}]},{"given":"Pedro M.","family":"Coutinho","sequence":"additional","affiliation":[{"name":"Architecture et Fonction des Macromol\u00e9cules Biologiques, UMR 7857 CNRS, Aix-Marseille University, F-13288 Marseille, France;"}]},{"given":"Bernard","family":"Henrissat","sequence":"additional","affiliation":[{"name":"Architecture et Fonction des Macromol\u00e9cules Biologiques, UMR 7857 CNRS, Aix-Marseille University, F-13288 Marseille, France;"},{"name":"Institut National de la Recherche Agronomique, USC 1408 Architecture et Fonction des Macromol\u00e9cules Biologiques, F-13288 Marseille, France,"},{"name":"Department of Biological Sciences, King Abdulaziz University, Jeddah, Saudi Arabia;"}]},{"given":"J. Paul","family":"Knox","sequence":"additional","affiliation":[{"name":"Centre for Plant Sciences, University of Leeds, Leeds LS2 9JT, United Kingdom"}]},{"given":"Arnaud","family":"Basl\u00e9","sequence":"additional","affiliation":[{"name":"Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom;"}]},{"given":"Shabir","family":"Najmudin","sequence":"additional","affiliation":[{"name":"Interdisciplinary Centre of Research in Animal Health, Faculdade de Medicina Veterin\u00e1ria, Universidade de Lisboa, P\u00f3lo Universit\u00e1rio do Alto da Ajuda, 1300-477 Lisbon, Portugal;"}]},{"given":"Harry J.","family":"Gilbert","sequence":"additional","affiliation":[{"name":"Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne NE2 4HH, United Kingdom;"}]},{"given":"William G. T.","family":"Willats","sequence":"additional","affiliation":[{"name":"Department of Plant and Environmental Sciences, Faculty of Science, University of Copenhagen, Copenhagen, Denmark;"}]},{"given":"Carlos M. G. A.","family":"Fontes","sequence":"additional","affiliation":[{"name":"Interdisciplinary Centre of Research in Animal Health, Faculdade de Medicina Veterin\u00e1ria, Universidade de Lisboa, P\u00f3lo Universit\u00e1rio do Alto da Ajuda, 1300-477 Lisbon, Portugal;"},{"name":"NZYTech Genes &amp; Enzymes, Campus do Lumiar, 1649-038 Lisbon, Portugal;"}]}],"member":"341","published-online":{"date-parts":[[2016,6,13]]},"reference":[{"key":"e_1_3_4_1_2","doi-asserted-by":"crossref","first-page":"444","DOI":"10.1104\/pp.110.156646","article-title":"The biochemistry and structural biology of plant cell wall deconstruction","volume":"153","author":"Gilbert HJ","year":"2010","unstructured":"HJ Gilbert, The biochemistry and structural biology of plant cell wall deconstruction. Plant Physiol 153, 444\u2013455 (2010).","journal-title":"Plant Physiol"},{"key":"e_1_3_4_2_2","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1128\/MMBR.69.1.124-154.2005","article-title":"Cellulase, clostridia, and ethanol","volume":"69","author":"Demain AL","year":"2005","unstructured":"AL Demain, M Newcomb, JH Wu, Cellulase, clostridia, and ethanol. Microbiol Mol Biol Rev 69, 124\u2013154 (2005).","journal-title":"Microbiol Mol Biol Rev"},{"key":"e_1_3_4_3_2","doi-asserted-by":"crossref","first-page":"669","DOI":"10.1016\/j.sbi.2013.05.005","article-title":"Advances in understanding the molecular basis of plant cell wall polysaccharide recognition by carbohydrate-binding modules","volume":"23","author":"Gilbert HJ","year":"2013","unstructured":"HJ Gilbert, JP Knox, AB Boraston, Advances in understanding the molecular basis of plant cell wall polysaccharide recognition by carbohydrate-binding modules. Curr Opin Struct Biol 23, 669\u2013677 (2013).","journal-title":"Curr Opin Struct Biol"},{"key":"e_1_3_4_4_2","doi-asserted-by":"crossref","first-page":"D490","DOI":"10.1093\/nar\/gkt1178","article-title":"The carbohydrate-active enzymes database (CAZy) in 2013","volume":"42","author":"Lombard V","year":"2014","unstructured":"V Lombard, H Golaconda Ramulu, E Drula, PM Coutinho, B Henrissat, The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res 42, D490\u2013D495 (2014).","journal-title":"Nucleic Acids Res"},{"key":"e_1_3_4_5_2","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1146\/annurev.micro.57.030502.091022","article-title":"The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides","volume":"58","author":"Bayer EA","year":"2004","unstructured":"EA Bayer, JP Belaich, Y Shoham, R Lamed, The cellulosomes: Multienzyme machines for degradation of plant cell wall polysaccharides. Annu Rev Microbiol 58, 521\u2013554 (2004).","journal-title":"Annu Rev Microbiol"},{"key":"e_1_3_4_6_2","doi-asserted-by":"crossref","first-page":"e12476","DOI":"10.1371\/journal.pone.0012476","article-title":"Abundance and diversity of dockerin-containing proteins in the fiber-degrading rumen bacterium, Ruminococcus flavefaciens FD-1","volume":"5","author":"Rincon MT","year":"2010","unstructured":"MT Rincon, , Abundance and diversity of dockerin-containing proteins in the fiber-degrading rumen bacterium, Ruminococcus flavefaciens FD-1. PLoS One 5, e12476 (2010).","journal-title":"PLoS One"},{"key":"e_1_3_4_7_2","doi-asserted-by":"crossref","first-page":"39429","DOI":"10.1074\/jbc.M112.396598","article-title":"Versatile high resolution oligosaccharide microarrays for plant glycobiology and cell wall research","volume":"287","author":"Pedersen HL","year":"2012","unstructured":"HL Pedersen, , Versatile high resolution oligosaccharide microarrays for plant glycobiology and cell wall research. J Biol Chem 287, 39429\u201339438 (2012).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_8_2","doi-asserted-by":"crossref","first-page":"1686","DOI":"10.1128\/AEM.03453-15","article-title":"Dividing the large glycoside hydrolase family 43 into subfamilies: A motivation for detailed enzyme characterization","volume":"82","author":"Mewis K","year":"2016","unstructured":"K Mewis, N Lenfant, V Lombard, B Henrissat, Dividing the large glycoside hydrolase family 43 into subfamilies: A motivation for detailed enzyme characterization. Appl Environ Microbiol 82, 1686\u20131692 (2016).","journal-title":"Appl Environ Microbiol"},{"key":"e_1_3_4_9_2","doi-asserted-by":"crossref","first-page":"5424","DOI":"10.1128\/JB.00503-10","article-title":"Domain analysis of a modular alpha-L-Arabinofuranosidase with a unique carbohydrate binding strategy from the fiber-degrading bacterium Fibrobacter succinogenes S85","volume":"192","author":"Yoshida S","year":"2010","unstructured":"S Yoshida, CW Hespen, RL Beverly, RI Mackie, IK Cann, Domain analysis of a modular alpha-L-Arabinofuranosidase with a unique carbohydrate binding strategy from the fiber-degrading bacterium Fibrobacter succinogenes S85. J Bacteriol 192, 5424\u20135436 (2010).","journal-title":"J Bacteriol"},{"key":"e_1_3_4_10_2","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1016\/S0008-6215(03)00079-X","article-title":"Structure of the xyloglucan produced by suspension-cultured tomato cells","volume":"338","author":"Jia Z","year":"2003","unstructured":"Z Jia, Q Qin, AG Darvill, WS York, Structure of the xyloglucan produced by suspension-cultured tomato cells. Carbohydr Res 338, 1197\u20131208 (2003).","journal-title":"Carbohydr Res"},{"key":"e_1_3_4_11_2","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1016\/j.jmb.2007.01.030","article-title":"Identification and characterization of a novel periplasmic polygalacturonic acid binding protein from Yersinia enterolitica","volume":"367","author":"Abbott DW","year":"2007","unstructured":"DW Abbott, S Hrynuik, AB Boraston, Identification and characterization of a novel periplasmic polygalacturonic acid binding protein from Yersinia enterolitica. J Mol Biol 367, 1023\u20131033 (2007).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_12_2","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1002\/(SICI)1521-1878(199802)20:2<156::AID-BIES8>3.0.CO;2-R","article-title":"Glycosaminoglycan-protein interactions: Definition of consensus sites in glycosaminoglycan binding proteins","volume":"20","author":"Hileman RE","year":"1998","unstructured":"RE Hileman, JR Fromm, JM Weiler, RJ Linhardt, Glycosaminoglycan-protein interactions: Definition of consensus sites in glycosaminoglycan binding proteins. BioEssays 20, 156\u2013167 (1998).","journal-title":"BioEssays"},{"key":"e_1_3_4_13_2","doi-asserted-by":"crossref","first-page":"41137","DOI":"10.1074\/jbc.M006948200","article-title":"The structural basis for the ligand specificity of family 2 carbohydrate-binding modules","volume":"275","author":"Simpson PJ","year":"2000","unstructured":"PJ Simpson, H Xie, DN Bolam, HJ Gilbert, MP Williamson, The structural basis for the ligand specificity of family 2 carbohydrate-binding modules. J Biol Chem 275, 41137\u201341142 (2000).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_14_2","doi-asserted-by":"crossref","first-page":"9316","DOI":"10.1021\/bi0347510","article-title":"Importance of hydrophobic and polar residues in ligand binding in the family 15 carbohydrate-binding module from Cellvibrio japonicus Xyn10C","volume":"42","author":"Pell G","year":"2003","unstructured":"G Pell, , Importance of hydrophobic and polar residues in ligand binding in the family 15 carbohydrate-binding module from Cellvibrio japonicus Xyn10C. Biochemistry 42, 9316\u20139323 (2003).","journal-title":"Biochemistry"},{"key":"e_1_3_4_15_2","doi-asserted-by":"crossref","first-page":"34665","DOI":"10.1074\/jbc.M110.168302","article-title":"Mutational insights into the roles of amino acid residues in ligand binding for two closely related family 16 carbohydrate binding modules","volume":"285","author":"Su X","year":"2010","unstructured":"X Su, , Mutational insights into the roles of amino acid residues in ligand binding for two closely related family 16 carbohydrate binding modules. J Biol Chem 285, 34665\u201334676 (2010).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_16_2","doi-asserted-by":"crossref","first-page":"5700","DOI":"10.1021\/bi010034z","article-title":"Role of hydrogen bonding in the interaction between a xylan binding module and xylan","volume":"40","author":"Xie H","year":"2001","unstructured":"H Xie, , Role of hydrogen bonding in the interaction between a xylan binding module and xylan. Biochemistry 40, 5700\u20135707 (2001).","journal-title":"Biochemistry"},{"key":"e_1_3_4_17_2","doi-asserted-by":"crossref","first-page":"12415","DOI":"10.1074\/jbc.M706513200","article-title":"Molecular basis for the selectivity and specificity of ligand recognition by the family 16 carbohydrate-binding modules from Thermoanaerobacterium polysaccharolyticum ManA","volume":"283","author":"Bae B","year":"2008","unstructured":"B Bae, , Molecular basis for the selectivity and specificity of ligand recognition by the family 16 carbohydrate-binding modules from Thermoanaerobacterium polysaccharolyticum ManA. J Biol Chem 283, 12415\u201312425 (2008).","journal-title":"J Biol Chem"},{"key":"e_1_3_4_18_2","doi-asserted-by":"crossref","first-page":"14077","DOI":"10.1073\/pnas.212516199","article-title":"Promiscuity in ligand-binding: The three-dimensional structure of a Piromyces carbohydrate-binding module, CBM29-2, in complex with cello- and mannohexaose","volume":"99","author":"Charnock SJ","year":"2002","unstructured":"SJ Charnock, , Promiscuity in ligand-binding: The three-dimensional structure of a Piromyces carbohydrate-binding module, CBM29-2, in complex with cello- and mannohexaose. Proc Natl Acad Sci USA 99, 14077\u201314082 (2002).","journal-title":"Proc Natl Acad Sci USA"},{"key":"e_1_3_4_19_2","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S0022-2860(00)00630-X","article-title":"A study of the conformation of beta-1,4-linked glucose oligomers, cellobiose to cellohexaose, in solution","volume":"556","author":"Sugiyama H","year":"2000","unstructured":"H Sugiyama, K Hisamichi, T Usui, K Sakai, J Ishiyama, A study of the conformation of beta-1,4-linked glucose oligomers, cellobiose to cellohexaose, in solution. J Mol Struct 556, 173\u2013177 (2000).","journal-title":"J Mol Struct"},{"key":"e_1_3_4_20_2","doi-asserted-by":"crossref","first-page":"1143","DOI":"10.1016\/S0022-2836(02)00374-1","article-title":"Differential oligosaccharide recognition by evolutionarily-related beta-1,4 and beta-1,3 glucan-binding modules","volume":"319","author":"Boraston AB","year":"2002","unstructured":"AB Boraston, , Differential oligosaccharide recognition by evolutionarily-related beta-1,4 and beta-1,3 glucan-binding modules. J Mol Biol 319, 1143\u20131156 (2002).","journal-title":"J Mol Biol"},{"key":"e_1_3_4_21_2","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1016\/S0014-5793(98)00625-5","article-title":"All three surface tryptophans in Type IIa cellulose binding domains play a pivotal role in binding both soluble and insoluble ligands","volume":"429","author":"Nagy T","year":"1998","unstructured":"T Nagy, , All three surface tryptophans in Type IIa cellulose binding domains play a pivotal role in binding both soluble and insoluble ligands. FEBS Lett 429, 312\u2013316 (1998).","journal-title":"FEBS Lett"},{"key":"e_1_3_4_22_2","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1042\/BJ20041473","article-title":"The interaction of carbohydrate-binding modules with insoluble non-crystalline cellulose is enthalpically driven","volume":"385","author":"Boraston AB","year":"2005","unstructured":"AB Boraston, The interaction of carbohydrate-binding modules with insoluble non-crystalline cellulose is enthalpically driven. Biochem J 385, 479\u2013484 (2005).","journal-title":"Biochem J"},{"key":"e_1_3_4_23_2","doi-asserted-by":"crossref","first-page":"5013","DOI":"10.1021\/bi992821q","article-title":"The X6 \u201cthermostabilizing\u201d domains of xylanases are carbohydrate-binding modules: Structure and biochemistry of the Clostridium thermocellum X6b domain","volume":"39","author":"Charnock SJ","year":"2000","unstructured":"SJ Charnock, , The X6 \u201cthermostabilizing\u201d domains of xylanases are carbohydrate-binding modules: Structure and biochemistry of the Clostridium thermocellum X6b domain. Biochemistry 39, 5013\u20135021 (2000).","journal-title":"Biochemistry"},{"key":"e_1_3_4_24_2","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"66","author":"Kabsch W","year":"2010","unstructured":"W Kabsch, XDS. Acta Crystallogr D Biol Crystallogr 66, 125\u2013132 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_25_2","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1107\/S0907444913000061","article-title":"How good are my data and what is the resolution?","volume":"69","author":"Evans PR","year":"2013","unstructured":"PR Evans, GN Murshudov, How good are my data and what is the resolution? Acta Crystallogr D Biol Crystallogr 69, 1204\u20131214 (2013).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_26_2","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1107\/S0907444909012098","article-title":"Decision-making in structure solution using Bayesian estimates of map quality: The PHENIX AutoSol wizard","volume":"65","author":"Terwilliger TC","year":"2009","unstructured":"TC Terwilliger, , Decision-making in structure solution using Bayesian estimates of map quality: The PHENIX AutoSol wizard. Acta Crystallogr D Biol Crystallogr 65, 582\u2013601 (2009).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_27_2","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy AJ","year":"2007","unstructured":"AJ McCoy, , Phaser crystallographic software. J Appl Cryst 40, 658\u2013674 (2007).","journal-title":"J Appl Cryst"},{"key":"e_1_3_4_28_2","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1107\/S0907444909038360","article-title":"Experimental phasing with SHELXC\/D\/E: Combining chain tracing with density modification","volume":"66","author":"Sheldrick GM","year":"2010","unstructured":"GM Sheldrick, Experimental phasing with SHELXC\/D\/E: Combining chain tracing with density modification. Acta Crystallogr D Biol Crystallogr 66, 479\u2013485 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_29_2","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley P","year":"2010","unstructured":"P Emsley, B Lohkamp, WG Scott, K Cowtan, Features and development of Coot. Acta Crystallogr D Biol Crystallogr 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_30_2","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1107\/S0907444911001314","article-title":"REFMAC5 for the refinement of macromolecular crystal structures","volume":"67","author":"Murshudov GN","year":"2011","unstructured":"GN Murshudov, , REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallogr D Biol Crystallogr 67, 355\u2013367 (2011).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_31_2","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","article-title":"Overview of the CCP4 suite and current developments","volume":"67","author":"Winn MD","year":"2011","unstructured":"MD Winn, , Overview of the CCP4 suite and current developments. Acta Crystallogr D Biol Crystallogr 67, 235\u2013242 (2011).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_32_2","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","article-title":"MolProbity: All-atom structure validation for macromolecular crystallography","volume":"66","author":"Chen VB","year":"2010","unstructured":"VB Chen, , MolProbity: All-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66, 12\u201321 (2010).","journal-title":"Acta Crystallogr D Biol Crystallogr"},{"key":"e_1_3_4_33_2","doi-asserted-by":"crossref","first-page":"22510","DOI":"10.1074\/jbc.M110.217315","article-title":"Structure and function of an arabinoxylan-specific xylanase","volume":"286","author":"Correia MA","year":"2011","unstructured":"MA Correia, , Structure and function of an arabinoxylan-specific xylanase. J Biol Chem 286, 22510\u201322520 (2011).","journal-title":"J Biol Chem"}],"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.pnas.org\/syndication\/doi\/10.1073\/pnas.1601558113","content-type":"unspecified","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.1601558113","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,6,7]],"date-time":"2022-06-07T14:38:30Z","timestamp":1654612710000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.1601558113"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,6,13]]},"references-count":33,"journal-issue":{"issue":"26","published-print":{"date-parts":[[2016,6,28]]}},"alternative-id":["10.1073\/pnas.1601558113"],"URL":"https:\/\/doi.org\/10.1073\/pnas.1601558113","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,6,13]]},"assertion":[{"value":"2016-06-13","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}