{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,10]],"date-time":"2026-02-10T19:36:00Z","timestamp":1770752160657,"version":"3.50.0"},"reference-count":64,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2017,4,1]],"date-time":"2017-04-01T00:00:00Z","timestamp":1491004800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100000780","name":"European Commission","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000780","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002923","name":"Consejo Nacional de Investigaciones Cient\u00edficas y T\u00e9cnicas","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100002923","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100010661","name":"Horizon 2020 Framework Programme","doi-asserted-by":"publisher","award":["653706"],"award-info":[{"award-number":["653706"]}],"id":[{"id":"10.13039\/100010661","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003074","name":"Agencia Nacional de Promoci\u00f3n Cient\u00edfica y Tecnol\u00f3gica","doi-asserted-by":"publisher","award":["PICT-2013-1629"],"award-info":[{"award-number":["PICT-2013-1629"]}],"id":[{"id":"10.13039\/501100003074","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004963","name":"Seventh Framework Programme","doi-asserted-by":"publisher","award":["283570"],"award-info":[{"award-number":["283570"]}],"id":[{"id":"10.13039\/501100004963","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100006589","name":"Ministry of Science and Technology, Croatia","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100006589","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100013060","name":"European Molecular Biology Laboratory","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100013060","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Molecular Biology"],"published-print":{"date-parts":[[2017,4]]},"DOI":"10.1016\/j.jmb.2016.12.022","type":"journal-article","created":{"date-parts":[[2017,1,12]],"date-time":"2017-01-12T08:45:17Z","timestamp":1484210717000},"page":"1192-1212","source":"Crossref","is-referenced-by-count":29,"title":["Three-Dimensional Structure of Full-Length NtrX, an Unusual Member of the NtrC Family of Response Regulators"],"prefix":"10.1016","volume":"429","author":[{"given":"Ignacio","family":"Fern\u00e1ndez","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Irina","family":"Cornaciu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mariela del Carmen","family":"Carrica","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Emiko","family":"Uchikawa","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Guillaume","family":"Hoffmann","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rodrigo","family":"Sieira","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jos\u00e9 Antonio","family":"M\u00e1rquez","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Fernando A.","family":"Goldbaum","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.jmb.2016.12.022_bb0005","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1146\/annurev.micro.091208.073214","article-title":"Biological insights from structures of two-component proteins","volume":"63","author":"Gao","year":"2009","journal-title":"Annu. Rev. Microbiol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0010","doi-asserted-by":"crossref","first-page":"1076","DOI":"10.1177\/0300985814540545","article-title":"Advancement of knowledge of Brucella over the past 50years","volume":"51","author":"Olsen","year":"2014","journal-title":"Vet. Pathol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0015","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1111\/j.1365-2958.2012.08095.x","article-title":"The NtrY\/X two-component system of Brucella spp. acts as a redox sensor and regulates the expression of nitrogen respiration enzymes","volume":"85","author":"Carrica","year":"2012","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0020","doi-asserted-by":"crossref","first-page":"222","DOI":"10.1111\/mmi.12181","article-title":"The two-component systems PrrBA and NtrYX coordinately regulate the adaptation of Brucella abortus to an oxygen-limited environment","volume":"88","author":"Carrica","year":"2013","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0025","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1007\/BF00293830","article-title":"Characterization of a novel Azorhizobium caulinodans ORS571 two-component regulatory system, NtrY\/NtrX, involved in nitrogen fixation and metabolism","volume":"231","author":"Pawlowski","year":"1991","journal-title":"Mol. Gen. Genet."},{"key":"10.1016\/j.jmb.2016.12.022_bb0030","doi-asserted-by":"crossref","first-page":"5014","DOI":"10.1128\/IAI.00735-06","article-title":"Biochemical activities of three pairs of Ehrlichia chaffeensis two-component regulatory system proteins involved in inhibition of lysosomal fusion","volume":"74","author":"Kumagai","year":"2006","journal-title":"Infect. Immun."},{"key":"10.1016\/j.jmb.2016.12.022_bb0035","doi-asserted-by":"crossref","DOI":"10.1128\/mBio.02141-14","article-title":"Ehrlichia chaffeensis proliferation begins with NtrY\/NtrX and PutA\/GlnA upregulation and CtrA degradation induced by proline and glutamine uptake","volume":"5","author":"Cheng","year":"2014","journal-title":"MBio"},{"key":"10.1016\/j.jmb.2016.12.022_bb0040","doi-asserted-by":"crossref","first-page":"2632","DOI":"10.1128\/JB.02062-12","article-title":"Characterization of an ntrX mutant of Neisseria gonorrhoeae reveals a response regulator that controls expression of respiratory enzymes in oxidase-positive proteobacteria","volume":"195","author":"Atack","year":"2013","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0045","doi-asserted-by":"crossref","first-page":"7150","DOI":"10.1128\/AEM.02225-13","article-title":"The Sinorhizobium meliloti ntrX gene is involved in succinoglycan production, motility, and symbiotic nodulation on alfalfa","volume":"79","author":"Wang","year":"2013","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0050","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.0030334","article-title":"Two-component signal transduction pathways regulating growth and cell cycle progression in a bacterium: a system-level analysis","volume":"3","author":"Skerker","year":"2005","journal-title":"PLoS Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0055","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1128\/MMBR.00006-12","article-title":"The role of bacterial enhancer binding proteins as specialized activators of \u03c354-dependent transcription","volume":"76","author":"Bush","year":"2012","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"10.1016\/j.jmb.2016.12.022_bb0060","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1038\/nrm1684","article-title":"AAA+ proteins: have engine, will work","volume":"6","author":"Hanson","year":"2005","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0065","doi-asserted-by":"crossref","first-page":"1884","DOI":"10.1101\/gad.12.12.1884","article-title":"A bacterial ATP-dependent, enhancer binding protein that activates the housekeeping RNA polymerase","volume":"12","author":"Bowman","year":"1998","journal-title":"Genes Dev."},{"key":"10.1016\/j.jmb.2016.12.022_bb0070","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1046\/j.1365-2958.1999.01660.x","article-title":"The synthesis of Rhodobacter capsulatus HupSL hydrogenase is regulated by the two-component HupT\/HupR system","volume":"34","author":"Dischert","year":"1999","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0075","doi-asserted-by":"crossref","first-page":"3258","DOI":"10.1016\/j.jmb.2015.06.010","article-title":"Snapshots of conformational changes shed light into the NtrX receiver domain signal transduction mechanism","volume":"427","author":"Fern\u00e1ndez","year":"2015","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0080","doi-asserted-by":"crossref","first-page":"454","DOI":"10.1107\/S2059798316000954","article-title":"Automated harvesting and processing of protein crystals through laser photoablation","volume":"72","author":"Zander","year":"2016","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0085","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/j.femsre.2004.12.008","article-title":"The many faces of the helix-turn-helix domain: transcription regulation and beyond","volume":"29","author":"Aravind","year":"2005","journal-title":"FEMS Microbiol. Rev."},{"key":"10.1016\/j.jmb.2016.12.022_bb0090","doi-asserted-by":"crossref","first-page":"3553","DOI":"10.1016\/j.jmb.2014.08.009","article-title":"DNA recognition by a \u03c3(54) transcriptional activator from Aquifex aeolicus","volume":"426","author":"Vidangos","year":"2014","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0095","doi-asserted-by":"crossref","first-page":"2256","DOI":"10.1107\/S0907444904026460","article-title":"Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions","volume":"60","author":"Krissinel","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.12.022_bb0100","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1101\/gad.1125603","article-title":"Regulation of the transcriptional activator NtrC1: structural studies of the regulatory and AAA+ ATPase domains","volume":"17","author":"Lee","year":"2003","journal-title":"Genes Dev."},{"key":"10.1016\/j.jmb.2016.12.022_bb0105","doi-asserted-by":"crossref","first-page":"1058","DOI":"10.1016\/j.jmb.2008.10.024","article-title":"Structure and regulatory mechanism of Aquifex aeolicus NtrC4: variability and evolution in bacterial transcriptional regulation","volume":"384","author":"Batchelor","year":"2008","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0110","doi-asserted-by":"crossref","first-page":"1326","DOI":"10.1096\/fj.00-0516fje","article-title":"A dimeric two-component receiver domain inhibits the sigma54-dependent ATPase in DctD","volume":"15","author":"Meyer","year":"2001","journal-title":"FASEB J."},{"key":"10.1016\/j.jmb.2016.12.022_bb0115","doi-asserted-by":"crossref","first-page":"774","DOI":"10.1016\/j.jmb.2007.05.022","article-title":"Inference of macromolecular assemblies from crystalline state","volume":"372","author":"Krissinel","year":"2007","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0120","doi-asserted-by":"crossref","first-page":"13,831","DOI":"10.1016\/S0021-9258(17)38800-2","article-title":"Photoaffinity labeling of the cap-binding protein complex with ATP\/dATP. Differential labeling of free eukaryotic initiation factor 4A and the eukaryotic initiation factor 4A component of the cap-binding protein complex with [alpha-32P]ATP\/dATP","volume":"260","author":"Sarkar","year":"1985","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2016.12.022_bb0125","doi-asserted-by":"crossref","first-page":"12,813","DOI":"10.1021\/bi035200c","article-title":"Novel destabilization of nucleotide binding by the gamma phosphate of ATP in the yeast SR protein kinase Sky1p","volume":"42","author":"Aubol","year":"2003","journal-title":"Biochemistry"},{"key":"10.1016\/j.jmb.2016.12.022_bb0130","doi-asserted-by":"crossref","first-page":"4628","DOI":"10.1128\/JB.181.15.4628-4638.1999","article-title":"MgATP binding and hydrolysis determinants of NtrC, a bacterial enhancer-binding protein","volume":"181","author":"Rombel","year":"1999","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0135","doi-asserted-by":"crossref","first-page":"34,997","DOI":"10.1074\/jbc.M606628200","article-title":"Heterogeneous nucleotide occupancy stimulates functionality of phage shock protein F, an AAA+ transcriptional activator","volume":"281","author":"Joly","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2016.12.022_bb0140","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1016\/0092-8674(91)90579-N","article-title":"The phosphorylated form of the enhancer-binding protein NTRC has an ATPase activity that is essential for activation of transcription","volume":"67","author":"Weiss","year":"1991","journal-title":"Cell"},{"key":"10.1016\/j.jmb.2016.12.022_bb0145","doi-asserted-by":"crossref","first-page":"246","DOI":"10.1016\/j.mib.2010.01.006","article-title":"Summary of useful methods for two-component system research","volume":"13","author":"Scharf","year":"2010","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0150","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.jmb.2008.10.027","article-title":"The HupR receiver domain crystal structure in its nonphospho and inhibitory phospho states","volume":"385","author":"Davies","year":"2009","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0155","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1016\/j.jmb.2005.12.052","article-title":"Structural basis of the nucleotide driven conformational changes in the AAA+ domain of transcription activator PspF","volume":"357","author":"Rappas","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0160","first-page":"126","article-title":"Bacterial regulatory networks include direct contact of response regulator proteins: interaction of RegA and NtrX in Rhodobacter capsulatus","volume":"13","author":"Gregor","year":"2007","journal-title":"J. Mol. Microbiol. Biotechnol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0165","doi-asserted-by":"crossref","first-page":"1849","DOI":"10.1038\/nprot.2007.249","article-title":"Electrophoretic mobility shift assay (EMSA) for detecting protein-nucleic acid interactions","volume":"2","author":"Hellman","year":"2007","journal-title":"Nat. Protoc."},{"key":"10.1016\/j.jmb.2016.12.022_bb0170","doi-asserted-by":"crossref","first-page":"1964","DOI":"10.1096\/fj.02-0395fje","article-title":"Two-component signaling in the AAA+ATPase DctD: binding Mg2+ and BeF3- selects between alternate dimeric states of the receiver domain","volume":"16","author":"Park","year":"2002","journal-title":"FASEB J."},{"key":"10.1016\/j.jmb.2016.12.022_bb0175","doi-asserted-by":"crossref","first-page":"242","DOI":"10.1016\/j.jmb.2005.08.003","article-title":"Negative regulation of AAA+ATPase assembly by two component receiver domains: a transcription activation mechanism that is conserved in mesophilic and extremely hyperthermophilic bacteria","volume":"353","author":"Doucleff","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0180","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.mib.2011.11.009","article-title":"Histidine kinases and response regulators in networks","volume":"15","author":"Jung","year":"2012","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0185","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.jmb.2006.02.072","article-title":"Structural and functional studies of the response regulator HupR","volume":"359","author":"Davies","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0190","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.bbamcr.2011.08.012","article-title":"Coupling AAA protein function to regulated gene expression","volume":"1823","author":"Joly","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.jmb.2016.12.022_bb0195","doi-asserted-by":"crossref","first-page":"1082","DOI":"10.1002\/bip.22333","article-title":"Structure, function, and tethering of DNA-binding domains in \u03c3(54) transcriptional activators","volume":"99","author":"Vidangos","year":"2013","journal-title":"Biopolymers"},{"key":"10.1016\/j.jmb.2016.12.022_bb0200","doi-asserted-by":"crossref","first-page":"3282","DOI":"10.1038\/ncomms4282","article-title":"An asymmetric heterodomain interface stabilizes a response regulator\u2013DNA complex","volume":"5","author":"Narayanan","year":"2014","journal-title":"Nat. Commun."},{"key":"10.1016\/j.jmb.2016.12.022_bb0205","doi-asserted-by":"crossref","first-page":"5088","DOI":"10.1073\/pnas.89.11.5088","article-title":"Phosphorylation of nitrogen regulator I of Escherichia coli induces strong cooperative binding to DNA essential for activation of transcription","volume":"89","author":"Weiss","year":"1992","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.jmb.2016.12.022_bb0210","doi-asserted-by":"crossref","first-page":"26,435","DOI":"10.1074\/jbc.271.42.26435","article-title":"Cooperative binding of DctD to the dctA upstream activation sequence of Rhizobium meliloti is enhanced in a constitutively active truncated mutant","volume":"271","author":"Scholl","year":"1996","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.jmb.2016.12.022_bb0215","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.mib.2004.02.011","article-title":"Regulation at complex bacterial promoters: how bacteria use different promoter organizations to produce different regulatory outcomes","volume":"7","author":"Barnard","year":"2004","journal-title":"Curr. Opin. Microbiol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0220","doi-asserted-by":"crossref","first-page":"771","DOI":"10.1038\/nsb845","article-title":"Dimerization allows DNA target site recognition by the NarL response regulator","volume":"9","author":"Maris","year":"2002","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0225","doi-asserted-by":"crossref","first-page":"302","DOI":"10.1038\/301302a0","article-title":"Positive control and autogenous regulation of the nifLA promoter in Klebsiella pneumoniae","volume":"301","author":"Drummond","year":"1983","journal-title":"Nature"},{"key":"10.1016\/j.jmb.2016.12.022_bb0230","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1002\/j.1460-2075.1984.tb01837.x","article-title":"Positive and negative control of the glnA ntrBC regulon in Klebsiella pneumoniae","volume":"3","author":"Alvarez-Morales","year":"1984","journal-title":"EMBO J."},{"key":"10.1016\/j.jmb.2016.12.022_bb0235","doi-asserted-by":"crossref","first-page":"305","DOI":"10.1111\/j.1365-2958.2010.07329.x","article-title":"Regulation of glutamate dehydrogenase expression in Pseudomonas putida results from its direct repression by NtrC under nitrogen-limiting conditions","volume":"78","author":"Herv\u00e1s","year":"2010","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0240","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1111\/j.1365-2958.2004.04385.x","article-title":"The TyrR regulon","volume":"55","author":"Pittard","year":"2005","journal-title":"Mol. Microbiol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0245","article-title":"Transcription of Ehrlichia chaffeensis genes is accomplished by RNA polymerase holoenzyme containing either sigma 32 or sigma 70","volume":"8","author":"Liu","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.jmb.2016.12.022_bb0250","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.jsb.2010.06.016","article-title":"Applications of the restriction free (RF) cloning procedure for molecular manipulations and protein expression","volume":"172","author":"Unger","year":"2010","journal-title":"J. Struct. Biol."},{"key":"10.1016\/j.jmb.2016.12.022_bb0255","doi-asserted-by":"crossref","unstructured":"E. Gasteiger, C. Hoogland, A. Gattiker, S. Duvaud, M.R. Wilkins, R.D. Appel, et al., Protein identification and analysis tools on the ExPASy server, In The Proteomics Protocols Handbook, Humana Press, Totowa, NJ, 2005: pp. 571\u2013607. doi:10.1385\/1-59259-890-0:571.","DOI":"10.1385\/1-59259-890-0:571"},{"key":"10.1016\/j.jmb.2016.12.022_bb0260","doi-asserted-by":"crossref","first-page":"204","DOI":"10.1107\/S1744309107004903","article-title":"Expression, crystallization and X-ray data collection from microcrystals of the extracellular domain of the human inhibitory receptor expressed on myeloid cells IREM-1","volume":"63","author":"Dimasi","year":"2007","journal-title":"Acta Crystallogr. F Struct. Biol. Cryst. Commun."},{"key":"10.1016\/j.jmb.2016.12.022_bb0265","doi-asserted-by":"crossref","first-page":"1393","DOI":"10.1107\/S0907444912031459","article-title":"CrystalDirect: a new method for automated crystal harvesting based on laser-induced photoablation of thin films","volume":"68","author":"Cipriani","year":"2012","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.12.022_bb0270","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1107\/S0909049512009715","article-title":"ID29: a high-intensity highly automated ESRF beamline for macromolecular crystallography experiments exploiting anomalous scattering","volume":"19","author":"de Sanctis","year":"2012","journal-title":"J. Synchrotron Radiat."},{"key":"10.1016\/j.jmb.2016.12.022_bb0275","doi-asserted-by":"crossref","first-page":"1757","DOI":"10.1107\/S1399004715011918","article-title":"Fully automatic characterization and data collection from crystals of biological macromolecules","volume":"71","author":"Svensson","year":"2015","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.12.022_bb0280","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1107\/S0907444909047337","article-title":"XDS","volume":"66","author":"Kabsch","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.12.022_bb0285","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","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.12.022_bb0290","doi-asserted-by":"crossref","first-page":"1002","DOI":"10.1107\/S0907444906022116","article-title":"The Buccaneer software for automated model building. 1. Tracing protein chains","volume":"62","author":"Cowtan","year":"2006","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.12.022_bb0295","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","article-title":"Phaser crystallographic software","volume":"40","author":"McCoy","year":"2007","journal-title":"J. Appl. Crystallogr."},{"key":"10.1016\/j.jmb.2016.12.022_bb0300","doi-asserted-by":"crossref","first-page":"368","DOI":"10.1107\/S0907444911056058","article-title":"Exploiting structure similarity in refinement: automated NCS and target-structure restraints in BUSTER","volume":"68","author":"Smart","year":"2012","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.12.022_bb0305","doi-asserted-by":"crossref","first-page":"2126","DOI":"10.1107\/S0907444904019158","article-title":"Coot: model-building tools for molecular graphics","volume":"60","author":"Emsley","year":"2004","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.12.022_bb0310","doi-asserted-by":"crossref","first-page":"897","DOI":"10.1016\/S0969-2126(96)00097-4","article-title":"Checking your imagination: applications of the free R value","volume":"4","author":"Kleywegt","year":"1996","journal-title":"Structure"},{"key":"10.1016\/j.jmb.2016.12.022_bb0315","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","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.jmb.2016.12.022_bb0320","doi-asserted-by":"crossref","first-page":"539","DOI":"10.1038\/msb.2011.75","article-title":"Fast, scalable generation of high-quality protein multiple sequence alignments using Clustal Omega","volume":"7","author":"Sievers","year":"2011","journal-title":"Mol. Syst. Biol."}],"container-title":["Journal of Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002228361730013X?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S002228361730013X?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,6,21]],"date-time":"2024-06-21T19:20:40Z","timestamp":1718997640000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S002228361730013X"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2017,4]]},"references-count":64,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2017,4]]}},"alternative-id":["S002228361730013X"],"URL":"https:\/\/doi.org\/10.1016\/j.jmb.2016.12.022","relation":{},"ISSN":["0022-2836"],"issn-type":[{"value":"0022-2836","type":"print"}],"subject":[],"published":{"date-parts":[[2017,4]]}}}