{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,10]],"date-time":"2026-04-10T09:57:58Z","timestamp":1775815078285,"version":"3.50.1"},"reference-count":53,"publisher":"Springer Science and Business Media LLC","issue":"12","license":[{"start":{"date-parts":[[2020,10,12]],"date-time":"2020-10-12T00:00:00Z","timestamp":1602460800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"},{"start":{"date-parts":[[2020,10,12]],"date-time":"2020-10-12T00:00:00Z","timestamp":1602460800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Struct Mol Biol"],"published-print":{"date-parts":[[2020,12]]},"DOI":"10.1038\/s41594-020-0510-9","type":"journal-article","created":{"date-parts":[[2020,10,12]],"date-time":"2020-10-12T12:07:04Z","timestamp":1602504424000},"page":"1142-1151","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["The structure of a calsequestrin filament reveals mechanisms of familial arrhythmia"],"prefix":"10.1038","volume":"27","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-6868-9121","authenticated-orcid":false,"given":"Erron W.","family":"Titus","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4454-6489","authenticated-orcid":false,"given":"Frederick H.","family":"Deiter","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chenxu","family":"Shi","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Julianne","family":"Wojciak","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Melvin","family":"Scheinman","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5129-641X","authenticated-orcid":false,"given":"Natalia","family":"Jura","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2791-9434","authenticated-orcid":false,"given":"Rahul C.","family":"Deo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2020,10,12]]},"reference":[{"key":"510_CR1","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1016\/j.yjmcc.2004.05.026","volume":"37","author":"DM Bers","year":"2004","unstructured":"Bers, D. M. Macromolecular complexes regulating cardiac ryanodine receptor function. J. Mol. Cell. Cardiol. 37, 417\u2013429 (2004).","journal-title":"J. Mol. Cell. Cardiol."},{"key":"510_CR2","doi-asserted-by":"crossref","first-page":"3101","DOI":"10.1113\/jphysiol.2009.171934","volume":"587","author":"L Royer","year":"2009","unstructured":"Royer, L. & R\u00edos, E. Deconstructing calsequestrin. Complex buffering in the calcium store of skeletal muscle. J. Physiol. 587, 3101\u20133111 (2009).","journal-title":"J. Physiol."},{"key":"510_CR3","doi-asserted-by":"crossref","unstructured":"Guerrero-Hern\u00e1ndez, A. et al. in Calcium Signaling (ed Islam, M. S.) 337\u2013370 (Springer International Publishing, 2020).","DOI":"10.1007\/978-3-030-12457-1_14"},{"key":"510_CR4","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1073\/pnas.68.6.1231","volume":"68","author":"DH MacLennan","year":"1971","unstructured":"MacLennan, D. H. & Wong, P. T. Isolation of a calcium-sequestering protein from sarcoplasmic reticulum. Proc. Natl Acad. Sci. USA 68, 1231\u20131235 (1971).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"510_CR5","doi-asserted-by":"crossref","first-page":"980","DOI":"10.1016\/S0021-9258(19)43027-5","volume":"249","author":"DH MacLennan","year":"1974","unstructured":"MacLennan, D. H. Isolation of a second form of calsequestrin. J. Biol. Chem. 249, 980\u2013984 (1974).","journal-title":"J. Biol. Chem."},{"key":"510_CR6","doi-asserted-by":"crossref","first-page":"974","DOI":"10.1016\/S0021-9258(19)43026-3","volume":"249","author":"TJ Ostwald","year":"1974","unstructured":"Ostwald, T. J. & MacLennan, D. H. Isolation of a high affinity calcium-binding protein from sarcoplasmic reticulum. J. Biol. Chem. 249, 974\u2013979 (1974).","journal-title":"J. Biol. Chem."},{"key":"510_CR7","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1083\/jcb.103.3.741","volume":"103","author":"B Costello","year":"1986","unstructured":"Costello, B. et al. Characterization of the junctional face membrane from terminal cisternae of sarcoplasmic reticulum. J. Cell Biol. 103, 741\u2013753 (1986).","journal-title":"J. Cell Biol."},{"key":"510_CR8","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1083\/jcb.105.1.49","volume":"105","author":"C Franzini-Armstrong","year":"1987","unstructured":"Franzini-Armstrong, C., Kenney, L. J. & Varriano-Marston, E. The structure of calsequestrin in triads of vertebrate skeletal muscle: a deep-etch study. J. Cell Biol. 105, 49\u201356 (1987).","journal-title":"J. Cell Biol."},{"key":"510_CR9","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1038\/nsb0698-476","volume":"5","author":"S Wang","year":"1998","unstructured":"Wang, S. et al. Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum. Nat. Struct. Biol. 5, 476\u2013483 (1998).","journal-title":"Nat. Struct. Biol."},{"key":"510_CR10","doi-asserted-by":"crossref","first-page":"18026","DOI":"10.1074\/jbc.M311553200","volume":"279","author":"H Park","year":"2004","unstructured":"Park, H. et al. Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization. J. Biol. Chem. 279, 18026\u201318033 (2004).","journal-title":"J. Biol. Chem."},{"key":"510_CR11","first-page":"2510","volume":"116","author":"BC Knollmann","year":"2006","unstructured":"Knollmann, B. C. et al. Casq2 deletion causes sarcoplasmic reticulum volume increase, premature Ca2+ release, and catecholaminergic polymorphic ventricular tachycardia. J. Clin. Invest. 116, 2510\u20132520 (2006).","journal-title":"J. Clin. Invest."},{"key":"510_CR12","doi-asserted-by":"crossref","first-page":"31358","DOI":"10.1074\/jbc.M113.507749","volume":"288","author":"S Perni","year":"2013","unstructured":"Perni, S., Close, M. & Franzini-Armstrong, C. Novel details of calsequestrin gel conformation in situ. J. Biol. Chem. 288, 31358\u201331362 (2013).","journal-title":"J. Biol. Chem."},{"key":"510_CR13","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/j.yexcr.2008.11.006","volume":"315","author":"ML Milstein","year":"2009","unstructured":"Milstein, M. L., Houle, T. D. & Cala, S. E. Calsequestrin isoforms localize to different ER sub-compartments: evidence for polymer and heteropolymer-dependent localization. Exp. Cell Res. 315, 523\u2013534 (2009).","journal-title":"Exp. Cell Res."},{"key":"510_CR14","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1016\/j.yjmcc.2010.05.012","volume":"49","author":"TP McFarland","year":"2010","unstructured":"McFarland, T. P., Milstein, M. L. & Cala, S. E. Rough endoplasmic reticulum to junctional sarcoplasmic reticulum trafficking of calsequestrin in adult cardiomyocytes. J. Mol. Cell. Cardiol. 49, 556\u2013564 (2010).","journal-title":"J. Mol. Cell. Cardiol."},{"key":"510_CR15","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1016\/j.yjmcc.2010.06.011","volume":"49","author":"BC Knollmann","year":"2010","unstructured":"Knollmann, B. C. A \u201crough\u201d journey to the sarcoplasmic reticulum\u2014implications of altered calsequestrin trafficking for cardiac arrhythmia. J. Mol. Cell. Cardiol. 49, 554\u2013555 (2010).","journal-title":"J. Mol. Cell. Cardiol."},{"key":"510_CR16","doi-asserted-by":"crossref","first-page":"3042","DOI":"10.1074\/jbc.M111.326363","volume":"287","author":"EJ Sanchez","year":"2012","unstructured":"Sanchez, E. J., Lewis, K. M., Munske, G. R., Nissen, M. S. & Kang, C. Glycosylation of skeletal calsequestrin: implications for its function. J. Biol. Chem. 287, 3042\u20133050 (2012).","journal-title":"J. Biol. Chem."},{"key":"510_CR17","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.yjmcc.2010.03.006","volume":"49","author":"U Kirchhefer","year":"2010","unstructured":"Kirchhefer, U. et al. The human CASQ2 mutation K206N is associated with hyperglycosylation and altered cellular calcium handling. J. Mol. Cell. Cardiol. 49, 95\u2013105 (2010).","journal-title":"J. Mol. Cell. Cardiol."},{"key":"510_CR18","doi-asserted-by":"crossref","first-page":"23389","DOI":"10.1074\/jbc.272.37.23389","volume":"272","author":"L Zhang","year":"1997","unstructured":"Zhang, L., Kelley, J., Schmeisser, G., Kobayashi, Y. M. & Jones, L. R. Complex formation between junctin, triadin, calsequestrin, and the ryanodine receptor. Proteins of the cardiac junctional sarcoplasmic reticulum membrane. J. Biol. Chem. 272, 23389\u201323397 (1997).","journal-title":"J. Biol. Chem."},{"key":"510_CR19","doi-asserted-by":"crossref","first-page":"149","DOI":"10.14348\/molcells.2016.2284","volume":"39","author":"S Rani","year":"2016","unstructured":"Rani, S., Park, C. S., Sreenivasaiah, P. K. & Kim, D. H. Characterization of Ca2+-dependent protein-protein interactions within the Ca2+ release units of cardiac sarcoplasmic reticulum. Mol. Cells 39, 149\u2013155 (2016).","journal-title":"Mol. Cells"},{"key":"510_CR20","doi-asserted-by":"crossref","unstructured":"Handhle, A. et al. Calsequestrin interacts directly with the cardiac ryanodine receptor luminal domain. J. Cell Sci. 129, 3983\u20133988 (2016).","DOI":"10.1242\/jcs.191643"},{"key":"510_CR21","doi-asserted-by":"crossref","first-page":"28665","DOI":"10.1074\/jbc.M115.686261","volume":"290","author":"KM Lewis","year":"2015","unstructured":"Lewis, K. M., Ronish, L. A., R\u00edos, E. & Kang, C. Characterization of two human skeletal calsequestrin mutants implicated in malignant hyperthermia and vacuolar aggregate myopathy. J. Biol. Chem. 290, 28665\u201328674 (2015).","journal-title":"J. Biol. Chem."},{"key":"510_CR22","doi-asserted-by":"crossref","first-page":"17188","DOI":"10.1074\/jbc.M109.096354","volume":"285","author":"NC Bal","year":"2010","unstructured":"Bal, N. C. et al. The catecholaminergic polymorphic ventricular tachycardia mutation R33Q disrupts the N-terminal structural motif that regulates reversible calsequestrin polymerization. J. Biol. Chem. 285, 17188\u201317196 (2010).","journal-title":"J. Biol. Chem."},{"key":"510_CR23","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1042\/BJ20101771","volume":"435","author":"NC Bal","year":"2011","unstructured":"Bal, N. C. et al. Probing cationic selectivity of cardiac calsequestrin and its CPVT mutants. Biochem. J. 435, 391\u2013399 (2011).","journal-title":"Biochem. J."},{"key":"510_CR24","doi-asserted-by":"crossref","first-page":"1652","DOI":"10.1016\/j.hrthm.2016.05.004","volume":"13","author":"B Gray","year":"2016","unstructured":"Gray, B. et al. A novel heterozygous mutation in cardiac calsequestrin causes autosomal dominant catecholaminergic polymorphic ventricular tachycardia. Heart Rhythm 13, 1652\u20131660 (2016).","journal-title":"Heart Rhythm"},{"key":"510_CR25","doi-asserted-by":"crossref","first-page":"1047","DOI":"10.1016\/j.jmb.2007.08.055","volume":"373","author":"E Kim","year":"2007","unstructured":"Kim, E. et al. Characterization of human cardiac calsequestrin and its deleterious mutants. J. Mol. Biol. 373, 1047\u20131057 (2007).","journal-title":"J. Mol. Biol."},{"key":"510_CR26","doi-asserted-by":"crossref","first-page":"11592","DOI":"10.1074\/jbc.M111.335075","volume":"287","author":"EJ Sanchez","year":"2012","unstructured":"Sanchez, E. J., Lewis, K. M., Danna, B. R. & Kang, C. High-capacity Ca2+ binding of human skeletal calsequestrin. J. Biol. Chem. 287, 11592\u201311601 (2012).","journal-title":"J. Biol. Chem."},{"key":"510_CR27","doi-asserted-by":"crossref","unstructured":"Lewis, K. M. et al. Characterization of post-translational modifications to calsequestrins of cardiac and skeletal muscle. Int. J. Mol. Sci. 17, 1539 (2016).","DOI":"10.3390\/ijms17091539"},{"key":"510_CR28","doi-asserted-by":"crossref","first-page":"9453","DOI":"10.1016\/S0021-9258(18)92842-5","volume":"266","author":"KH Krause","year":"1991","unstructured":"Krause, K. H., Milos, M., Luan-Rilliet, Y., Lew, D. P. & Cox, J. A. Thermodynamics of cation binding to rabbit skeletal muscle calsequestrin. Evidence for distinct Ca2+- and Mg2+-binding sites. J. Biol. Chem. 266, 9453\u20139459 (1991).","journal-title":"J. Biol. Chem."},{"key":"510_CR29","doi-asserted-by":"crossref","first-page":"79","DOI":"10.1038\/295079a0","volume":"295","author":"L Sawyer","year":"1982","unstructured":"Sawyer, L. & James, M. N. G. Carboxyl\u2013carboxylate interactions in proteins. Nature 295, 79\u201380 (1982).","journal-title":"Nature"},{"key":"510_CR30","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1038\/nature05959","volume":"448","author":"KK Frederick","year":"2007","unstructured":"Frederick, K. K., Marlow, M. S., Valentine, K. G. & Wand, A. J. Conformational entropy in molecular recognition by proteins. Nature 448, 325\u2013329 (2007).","journal-title":"Nature"},{"key":"510_CR31","doi-asserted-by":"crossref","first-page":"6279","DOI":"10.1021\/bi00368a067","volume":"25","author":"M Milos","year":"1986","unstructured":"Milos, M., Schaer, J. J., Comte, M. & Cox, J. A. Calcium\u2013proton and calcium-magnesium antagonisms in calmodulin: microcalorimetric and potentiometric analyses. Biochemistry 25, 6279\u20136287 (1986).","journal-title":"Biochemistry"},{"key":"510_CR32","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1016\/S0006-3495(98)77786-0","volume":"74","author":"F Kamp","year":"1998","unstructured":"Kamp, F., Donoso, P. & Hidalgo, C. Changes in luminal pH caused by calcium release in sarcoplasmic reticulum vesicles. Biophys. J. 74, 290\u2013296 (1998).","journal-title":"Biophys. J."},{"key":"510_CR33","doi-asserted-by":"crossref","first-page":"2130","DOI":"10.1016\/S0006-3495(96)79413-4","volume":"71","author":"C Hidalgo","year":"1996","unstructured":"Hidalgo, C., Donoso, P. & Rodriguez, P. H. Protons induce calsequestrin conformational changes. Biophys. J. 71, 2130\u20132137 (1996).","journal-title":"Biophys. J."},{"key":"510_CR34","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1107\/S2059798317017235","volume":"74","author":"G Winter","year":"2018","unstructured":"Winter, G. et al. DIALS: implementation and evaluation of a new integration package. Acta Crystallogr D Struct. Biol. 74, 85\u201397 (2018).","journal-title":"Acta Crystallogr D Struct. Biol."},{"key":"510_CR35","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1107\/S0021889809045701","volume":"43","author":"G Winter","year":"2010","unstructured":"Winter, G. xia2: an expert system for macromolecular crystallography data reduction. J. Appl. Crystallogr. 43, 186\u2013190 (2010).","journal-title":"J. Appl. Crystallogr."},{"key":"510_CR36","doi-asserted-by":"crossref","first-page":"1204","DOI":"10.1107\/S0907444913000061","volume":"69","author":"PR Evans","year":"2013","unstructured":"Evans, P. R. & Murshudov, G. N. 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":"510_CR37","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1107\/S0907444905036693","volume":"62","author":"P Evans","year":"2006","unstructured":"Evans, P. Scaling and assessment of data quality. Acta Crystallogr. D Biol. Crystallogr. 62, 72\u201382 (2006).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"510_CR38","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1107\/S0907444910045749","volume":"67","author":"MD Winn","year":"2011","unstructured":"Winn, M. D. et al. 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":"510_CR39","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1107\/S0021889807021206","volume":"40","author":"AJ McCoy","year":"2007","unstructured":"McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658\u2013674 (2007).","journal-title":"J. Appl. Crystallogr."},{"key":"510_CR40","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"PD Adams","year":"2010","unstructured":"Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213\u2013221 (2010).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"510_CR41","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1107\/S0907444912001308","volume":"68","author":"PV Afonine","year":"2012","unstructured":"Afonine, P. V. et al. Towards automated crystallographic structure refinement with phenix.refine. Acta Crystallogr. D Biol. Crystallogr. 68, 352\u2013367 (2012).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"510_CR42","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1107\/S0909049503023938","volume":"11","author":"T Terwilliger","year":"2004","unstructured":"Terwilliger, T. SOLVE and RESOLVE: automated structure solution, density modification and model building. J. Synchrotron Radiat. 11, 49\u201352 (2004).","journal-title":"J. Synchrotron Radiat."},{"key":"510_CR43","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1107\/S090744490705024X","volume":"64","author":"TC Terwilliger","year":"2008","unstructured":"Terwilliger, T. C. et al. Iterative model building, structure refinement and density modification with the PHENIX AutoBuild wizard. Acta Crystallogr. D Biol. Crystallogr. 64, 61\u201369 (2008).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"510_CR44","first-page":"27","volume":"43","author":"PH Zwart","year":"2005","unstructured":"Zwart, P. H., Grosse-Kunstleve, R. W. & Adams, P. D. Xtriage and Fest: automatic assessment of X-ray data and substructure structure factor estimation. CCP4 Newsl. 43, 27\u201335 (2005).","journal-title":"CCP4 Newsl."},{"key":"510_CR45","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","volume":"66","author":"P Emsley","year":"2010","unstructured":"Emsley, P., Lohkamp, B., Scott, W. G. & Cowtan, K. Features and development of Coot. Acta Crystallogr. D Biol. Crystallogr. 66, 486\u2013501 (2010).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"510_CR46","doi-asserted-by":"crossref","first-page":"2430","DOI":"10.1107\/S1399004714014795","volume":"70","author":"AA Lebedev","year":"2014","unstructured":"Lebedev, A. A. & Isupov, M. N. Space-group and origin ambiguity in macromolecular structures with pseudo-symmetry and its treatment with the program Zanuda. Acta Crystallogr. D Biol. Crystallogr. 70, 2430\u20132443 (2014).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"510_CR47","doi-asserted-by":"crossref","first-page":"W665","DOI":"10.1093\/nar\/gkh381","volume":"32","author":"TJ Dolinsky","year":"2004","unstructured":"Dolinsky, T. J., Nielsen, J. E., McCammon, J. A. & Baker, N. A. PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res. 32, W665\u2013W667 (2004).","journal-title":"Nucleic Acids Res."},{"key":"510_CR48","doi-asserted-by":"crossref","first-page":"5179","DOI":"10.1021\/ja00124a002","volume":"117","author":"WD Cornell","year":"1995","unstructured":"Cornell, W. D. et al. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 117, 5179\u20135197 (1995).","journal-title":"J. Am. Chem. Soc."},{"key":"510_CR49","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1002\/pro.3280","volume":"27","author":"E Jurrus","year":"2018","unstructured":"Jurrus, E. et al. Improvements to the APBS biomolecular solvation software suite. Protein Sci. 27, 112\u2013128 (2018).","journal-title":"Protein Sci."},{"key":"510_CR50","unstructured":"Schr\u00f6dinger, LLC. The PyMOL Molecular Graphics System, Version 2.2.3 (2019)."},{"key":"510_CR51","volume":"8","author":"BK Ho","year":"2008","unstructured":"Ho, B. K. & Gruswitz, F. HOLLOW: generating accurate representations of channel and interior surfaces in molecular structures. BMC Struct. Biol. 8, 49 (2008).","journal-title":"BMC Struct. Biol."},{"key":"510_CR52","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1093\/bioinformatics\/16.2.135","volume":"16","author":"E Beitz","year":"2000","unstructured":"Beitz, E. TeXshade: shading and labeling of multiple sequence alignments using LaTeX2e. Bioinformatics 16, 135\u2013139 (2000).","journal-title":"Bioinformatics"},{"key":"510_CR53","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1109\/MCSE.2007.55","volume":"9","author":"JD Hunter","year":"2007","unstructured":"Hunter, J. D. Matplotlib: a 2D graphics environment. Comput. Sci. Eng. 9, 90\u201395 (2007).","journal-title":"Comput. Sci. Eng."}],"container-title":["Nature Structural &amp; Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41594-020-0510-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41594-020-0510-9","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41594-020-0510-9.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,10,11]],"date-time":"2021-10-11T22:09:35Z","timestamp":1633990175000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41594-020-0510-9"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,10,12]]},"references-count":53,"journal-issue":{"issue":"12","published-print":{"date-parts":[[2020,12]]}},"alternative-id":["510"],"URL":"https:\/\/doi.org\/10.1038\/s41594-020-0510-9","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/672303","asserted-by":"object"}]},"ISSN":["1545-9993","1545-9985"],"issn-type":[{"value":"1545-9993","type":"print"},{"value":"1545-9985","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,10,12]]},"assertion":[{"value":"25 July 2019","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"19 August 2020","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"12 October 2020","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}