{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,26]],"date-time":"2026-03-26T06:49:23Z","timestamp":1774507763141,"version":"3.50.1"},"reference-count":61,"publisher":"Springer Science and Business Media LLC","issue":"7607","license":[{"start":{"date-parts":[[2016,5,18]],"date-time":"2016-05-18T00:00:00Z","timestamp":1463529600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nature"],"published-print":{"date-parts":[[2016,6]]},"DOI":"10.1038\/nature17964","type":"journal-article","created":{"date-parts":[[2016,5,17]],"date-time":"2016-05-17T12:42:05Z","timestamp":1463488925000},"page":"347-351","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":791,"title":["TRPV1 structures in nanodiscs reveal mechanisms of ligand and lipid action"],"prefix":"10.1038","volume":"534","author":[{"given":"Yuan","family":"Gao","sequence":"first","affiliation":[]},{"given":"Erhu","family":"Cao","sequence":"additional","affiliation":[]},{"given":"David","family":"Julius","sequence":"additional","affiliation":[]},{"given":"Yifan","family":"Cheng","sequence":"additional","affiliation":[]}],"member":"297","published-online":{"date-parts":[[2016,5,18]]},"reference":[{"key":"BFnature17964_CR1","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1146\/annurev.physiol.65.092101.142453","volume":"65","author":"DW Hilgemann","year":"2003","unstructured":"Hilgemann, D. W. Getting ready for the decade of the lipids. Annu. Rev. Physiol. 65, 697\u2013700 (2003)","journal-title":"Annu. Rev. Physiol."},{"key":"BFnature17964_CR2","doi-asserted-by":"crossref","first-page":"844","DOI":"10.1016\/j.bbalip.2014.09.010","volume":"1851","author":"B Hille","year":"2015","unstructured":"Hille, B., Dickson, E. J., Kruse, M., Vivas, O. & Suh, B. C. Phosphoinositides regulate ion channels. Biochim. Biophys. Acta 1851, 844\u2013856 (2015)","journal-title":"Biochim. Biophys. Acta"},{"key":"BFnature17964_CR3","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1016\/j.tibs.2011.06.007","volume":"36","author":"AG Lee","year":"2011","unstructured":"Lee, A. G. Biological membranes: the importance of molecular detail. Trends Biochem. Sci. 36, 493\u2013500 (2011)","journal-title":"Trends Biochem. Sci."},{"key":"BFnature17964_CR4","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1016\/S0959-440X(00)00119-6","volume":"10","author":"M Caffrey","year":"2000","unstructured":"Caffrey, M. A lipid\u2019s eye view of membrane protein crystallization in mesophases. Curr. Opin. Struct. Biol. 10, 486\u2013497 (2000)","journal-title":"Curr. Opin. Struct. Biol."},{"key":"BFnature17964_CR5","doi-asserted-by":"crossref","first-page":"14532","DOI":"10.1073\/pnas.93.25.14532","volume":"93","author":"EM Landau","year":"1996","unstructured":"Landau, E. M. & Rosenbusch, J. P. Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc. Natl Acad. Sci. USA 93, 14532\u201314535 (1996)","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"BFnature17964_CR6","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1038\/nature04321","volume":"438","author":"T Gonen","year":"2005","unstructured":"Gonen, T. et al. Lipid-protein interactions in double-layered two-dimensional AQP0 crystals. Nature 438, 633\u2013638 (2005)","journal-title":"Nature"},{"key":"BFnature17964_CR7","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1038\/nature08291","volume":"461","author":"L Wang","year":"2009","unstructured":"Wang, L. & Sigworth, F. J. Structure of the BK potassium channel in a lipid membrane from electron cryomicroscopy. Nature 461, 292\u2013295 (2009)","journal-title":"Nature"},{"key":"BFnature17964_CR8","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1021\/nl025623k","volume":"2","author":"TH Bayburt","year":"2002","unstructured":"Bayburt, T. H., Grinkova, Y. V. & Sligar, S. G. Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins. Nano Lett. 2, 853\u2013856 (2002)","journal-title":"Nano Lett."},{"key":"BFnature17964_CR9","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1016\/j.jmb.2008.01.066","volume":"377","author":"S Banerjee","year":"2008","unstructured":"Banerjee, S., Huber, T. & Sakmar, T. P. Rapid incorporation of functional rhodopsin into nanoscale apolipoprotein bound bilayer (NABB) particles. J. Mol. Biol. 377, 1067\u20131081 (2008)","journal-title":"J. Mol. Biol."},{"key":"BFnature17964_CR10","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/S0076-6879(09)64011-8","volume":"464","author":"TK Ritchie","year":"2009","unstructured":"Ritchie, T. K. et al. Reconstitution of membrane proteins in phospholipid bilayer nanodiscs. Methods Enzymol. 464, 211\u2013231 (2009)","journal-title":"Methods Enzymol."},{"key":"BFnature17964_CR11","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1038\/nature13916","volume":"517","author":"RG Efremov","year":"2015","unstructured":"Efremov, R. G., Leitner, A., Aebersold, R. & Raunser, S. Architecture and conformational switch mechanism of the ryanodine receptor. Nature 517, 39\u201343 (2015)","journal-title":"Nature"},{"key":"BFnature17964_CR12","doi-asserted-by":"crossref","first-page":"614","DOI":"10.1038\/nsmb.2026","volume":"18","author":"J Frauenfeld","year":"2011","unstructured":"Frauenfeld, J. et al. Cryo-EM structure of the ribosome\u2013SecYE complex in the membrane environment. Nature Struct. Mol. Biol. 18, 614\u2013621 (2011)","journal-title":"Nature Struct. Mol. Biol."},{"key":"BFnature17964_CR13","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.tibs.2014.10.005","volume":"40","author":"XC Bai","year":"2015","unstructured":"Bai, X. C., McMullan, G. & Scheres, S. H. How cryo-EM is revolutionizing structural biology. Trends Biochem. Sci. 40, 49\u201357 (2015)","journal-title":"Trends Biochem. Sci."},{"key":"BFnature17964_CR14","doi-asserted-by":"crossref","first-page":"450","DOI":"10.1016\/j.cell.2015.03.049","volume":"161","author":"Y Cheng","year":"2015","unstructured":"Cheng, Y. Single-particle cryo-EM at crystallographic resolution. Cell 161, 450\u2013457 (2015)","journal-title":"Cell"},{"key":"BFnature17964_CR15","doi-asserted-by":"crossref","first-page":"e03678","DOI":"10.7554\/eLife.03678","volume":"3","author":"W K\u00fchlbrandt","year":"2014","unstructured":"K\u00fchlbrandt, W. Cryo-EM enters a new era. eLife 3, e03678 (2014)","journal-title":"eLife"},{"key":"BFnature17964_CR16","first-page":"207","volume":"222","author":"S Bevan","year":"2014","unstructured":"Bevan, S., Quallo, T. & Andersson, D. A. Trpv1. Handb. Exp. Pharmacol. 222, 207\u2013245 (2014)","journal-title":"Exp. Pharmacol."},{"key":"BFnature17964_CR17","doi-asserted-by":"crossref","first-page":"355","DOI":"10.1146\/annurev-cellbio-101011-155833","volume":"29","author":"D Julius","year":"2013","unstructured":"Julius, D. TRP channels and pain. Annu. Rev. Cell Dev. Biol. 29, 355\u2013384 (2013)","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"BFnature17964_CR18","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1038\/nature12823","volume":"504","author":"E Cao","year":"2013","unstructured":"Cao, E., Liao, M., Cheng, Y. & Julius, D. TRPV1 structures in distinct conformations reveal activation mechanisms. Nature 504, 113\u2013118 (2013)","journal-title":"Nature"},{"key":"BFnature17964_CR19","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1038\/nature12822","volume":"504","author":"M Liao","year":"2013","unstructured":"Liao, M., Cao, E., Julius, D. & Cheng, Y. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504, 107\u2013112 (2013)","journal-title":"Nature"},{"key":"BFnature17964_CR20","doi-asserted-by":"crossref","first-page":"376","DOI":"10.1038\/nature06265","volume":"450","author":"SB Long","year":"2007","unstructured":"Long, S. B., Tao, X., Campbell, E. B. & MacKinnon, R. Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Nature 450, 376\u2013382 (2007)","journal-title":"Nature"},{"key":"BFnature17964_CR21","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1016\/0306-4522(89)90269-8","volume":"30","author":"A Szallasi","year":"1989","unstructured":"Szallasi, A. & Blumberg, P. M. Resiniferatoxin, a phorbol-related diterpene, acts as an ultrapotent analog of capsaicin, the irritant constituent in red pepper. Neuroscience 30, 515\u2013520 (1989)","journal-title":"Neuroscience"},{"key":"BFnature17964_CR22","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1016\/j.cell.2010.03.052","volume":"141","author":"CJ Bohlen","year":"2010","unstructured":"Bohlen, C. J. et al. A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain. Cell 141, 834\u2013845 (2010)","journal-title":"Cell"},{"key":"BFnature17964_CR23","doi-asserted-by":"crossref","first-page":"2501","DOI":"10.1021\/bi035981h","volume":"43","author":"MZ Chou","year":"2004","unstructured":"Chou, M. Z., Mtui, T., Gao, Y. D., Kohler, M. & Middleton, R. E. Resiniferatoxin binds to the capsaicin receptor (TRPV1) near the extracellular side of the S4 transmembrane domain. Biochemistry 43, 2501\u20132511 (2004)","journal-title":"Biochemistry"},{"key":"BFnature17964_CR24","doi-asserted-by":"crossref","first-page":"20283","DOI":"10.1074\/jbc.M312577200","volume":"279","author":"NR Gavva","year":"2004","unstructured":"Gavva, N. R. et al. Molecular determinants of vanilloid sensitivity in TRPV1. J. Biol. Chem. 279, 20283\u201320295 (2004)","journal-title":"J. Biol. Chem."},{"key":"BFnature17964_CR25","doi-asserted-by":"crossref","first-page":"1425","DOI":"10.1016\/j.bpj.2015.02.013","volume":"108","author":"SM Hanson","year":"2015","unstructured":"Hanson, S. M., Newstead, S., Swartz, K. J. & Sansom, M. S. P. Capsaicin interaction with TRPV1 channels in a lipid bilayer: molecular dynamics simulation. Biophys. J. 108, 1425\u20131434 (2015)","journal-title":"Biophys. J."},{"key":"BFnature17964_CR26","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/S0092-8674(02)00637-2","volume":"108","author":"SE Jordt","year":"2002","unstructured":"Jordt, S. E. & Julius, D. Molecular basis for species-specific sensitivity to \u201chot\u201d chili peppers. Cell 108, 421\u2013430 (2002)","journal-title":"Cell"},{"key":"BFnature17964_CR27","doi-asserted-by":"crossref","first-page":"17165","DOI":"10.1074\/jbc.M313328200","volume":"279","author":"E Phillips","year":"2004","unstructured":"Phillips, E., Reeve, A., Bevan, S. & McIntyre, P. Identification of species-specific determinants of the action of the antagonist capsazepine and the agonist PPAHV on TRPV1. J. Biol. Chem. 279, 17165\u201317172 (2004)","journal-title":"J. Biol. Chem."},{"key":"BFnature17964_CR28","doi-asserted-by":"crossref","first-page":"518","DOI":"10.1038\/nchembio.1835","volume":"11","author":"F Yang","year":"2015","unstructured":"Yang, F. et al. Structural mechanism underlying capsaicin binding and activation of the TRPV1 ion channel. Nat. Chem. Biol. 11, 518\u2013524 (2015)","journal-title":"Nat. Chem. Biol."},{"key":"BFnature17964_CR29","doi-asserted-by":"crossref","first-page":"544","DOI":"10.1111\/j.1476-5381.1992.tb12781.x","volume":"107","author":"S Bevan","year":"1992","unstructured":"Bevan, S. et al. Capsazepine: a competitive antagonist of the sensory neurone excitant capsaicin. Br. J. Pharmacol. 107, 544\u2013552 (1992)","journal-title":"Br. J. Pharmacol."},{"key":"BFnature17964_CR30","doi-asserted-by":"crossref","first-page":"41455","DOI":"10.1074\/jbc.M110.145466","volume":"285","author":"S Boukalova","year":"2010","unstructured":"Boukalova, S., Marsakova, L., Teisinger, J. & Vlachova, V. Conserved residues within the putative S4-S5 region serve distinct functions among thermosensitive vanilloid transient receptor potential (TRPV) channels. J. Biol. Chem. 285, 41455\u201341462 (2010)","journal-title":"J. Biol. Chem."},{"key":"BFnature17964_CR31","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1038\/nature02632","volume":"430","author":"SY Lee","year":"2004","unstructured":"Lee, S. Y. & MacKinnon, R. A membrane-access mechanism of ion channel inhibition by voltage sensor toxins from spider venom. Nature 430, 232\u2013235 (2004)","journal-title":"Nature"},{"key":"BFnature17964_CR32","doi-asserted-by":"crossref","first-page":"1080","DOI":"10.1038\/nsmb.1679","volume":"16","author":"M Milescu","year":"2009","unstructured":"Milescu, M. et al. Interactions between lipids and voltage sensor paddles detected with tarantula toxins. Nature Struct. Mol. Biol. 16, 1080\u20131085 (2009)","journal-title":"Nature Struct. Mol. Biol."},{"key":"BFnature17964_CR33","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1085\/jgp.200709869","volume":"130","author":"M Milescu","year":"2007","unstructured":"Milescu, M. et al. Tarantula toxins interact with voltage sensors within lipid membranes. J. Gen. Physiol. 130, 497\u2013511 (2007)","journal-title":"J. Gen. Physiol."},{"key":"BFnature17964_CR34","doi-asserted-by":"crossref","first-page":"e11273","DOI":"10.7554\/eLife.11273","volume":"5","author":"C Bae","year":"2016","unstructured":"Bae, C. et al. Structural insights into the mechanism of activation of the TRPV1 channel by a membrane-bound tarantula toxin. eLife 5, e11273 (2016)","journal-title":"eLife"},{"key":"BFnature17964_CR35","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1113\/jphysiol.2006.118372","volume":"578","author":"RC Hardie","year":"2007","unstructured":"Hardie, R. C. TRP channels and lipids: from Drosophila to mammalian physiology. J. Physiol. 578, 9\u201324 (2007)","journal-title":"J. Physiol."},{"key":"BFnature17964_CR36","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1007\/978-3-540-34891-7_30","volume":"179","author":"F Qin","year":"2007","unstructured":"Qin, F. Regulation of TRP ion channels by phosphatidylinositol-4,5-bisphosphate. Handb. Exp. Pharmacol. 179, 509\u2013525 (2007)","journal-title":"Handb. Exp. Pharmacol."},{"key":"BFnature17964_CR37","doi-asserted-by":"crossref","first-page":"1851","DOI":"10.1007\/s00424-015-1695-3","volume":"467","author":"T Rohacs","year":"2015","unstructured":"Rohacs, T. Phosphoinositide regulation of TRPV1 revisited. Pflugers Arch. 467, 1851\u20131869 (2015)","journal-title":"Pflugers Arch."},{"key":"BFnature17964_CR38","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1016\/j.neuron.2012.12.016","volume":"77","author":"E Cao","year":"2013","unstructured":"Cao, E., Cordero-Morales, J. F., Liu, B., Qin, F. & Julius, D. TRPV1 channels are intrinsically heat sensitive and negatively regulated by phosphoinositide lipids. Neuron 77, 667\u2013679 (2013)","journal-title":"Neuron"},{"key":"BFnature17964_CR39","doi-asserted-by":"crossref","first-page":"1284","DOI":"10.1126\/science.1083646","volume":"300","author":"ED Prescott","year":"2003","unstructured":"Prescott, E. D. & Julius, D. A modular PIP2 binding site as a determinant of capsaicin receptor sensitivity. Science 300, 1284\u20131288 (2003)","journal-title":"Science"},{"key":"BFnature17964_CR40","doi-asserted-by":"crossref","first-page":"431","DOI":"10.1085\/jgp.201511354","volume":"145","author":"CA Ufret-Vincenty","year":"2015","unstructured":"Ufret-Vincenty, C. A. et al. Mechanism for phosphoinositide selectivity and activation of TRPV1 ion channels. J. Gen. Physiol. 145, 431\u2013442 (2015)","journal-title":"J. Gen. Physiol."},{"key":"BFnature17964_CR41","doi-asserted-by":"crossref","first-page":"9688","DOI":"10.1074\/jbc.M110.192526","volume":"286","author":"CA Ufret-Vincenty","year":"2011","unstructured":"Ufret-Vincenty, C. A., Klein, R. M., Hua, L., Angueyra, J. & Gordon, S. E. Localization of the PIP2 sensor of TRPV1 ion channels. J. Biol. Chem. 286, 9688\u20139698 (2011)","journal-title":"J. Biol. Chem."},{"key":"BFnature17964_CR42","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1038\/nature10370","volume":"477","author":"SB Hansen","year":"2011","unstructured":"Hansen, S. B., Tao, X. & MacKinnon, R. Structural basis of PIP2 activation of the classical inward rectifier K+ channel Kir2.2. Nature 477, 495\u2013498 (2011)","journal-title":"Nature"},{"key":"BFnature17964_CR43","first-page":"3227","volume":"58","author":"DS Booth","year":"2011","unstructured":"Booth, D. S., Avila-Sakar, A. & Cheng, Y. Visualizing proteins and macromolecular complexes by negative stain EM: from grid preparation to image acquisition. J. Vis. Exp. 58, 3227 (2011)","journal-title":"J. Vis. Exp."},{"key":"BFnature17964_CR44","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1038\/nmeth.2472","volume":"10","author":"X Li","year":"2013","unstructured":"Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nature Methods 10, 584\u2013590 (2013)","journal-title":"Nature Methods"},{"key":"BFnature17964_CR45","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.jsb.2015.09.003","volume":"192","author":"X Li","year":"2015","unstructured":"Li, X., Zheng, S., Agard, D. A. & Cheng, Y. Asynchronous data acquisition and on-the-fly analysis of dose fractionated cryoEM images by UCSFImage. J. Struct. Biol. 192, 174\u2013178 (2015)","journal-title":"J. Struct. Biol."},{"key":"BFnature17964_CR46","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.jsb.2015.08.008","volume":"192","author":"A Rohou","year":"2015","unstructured":"Rohou, A. & Grigorieff, N. CTFFIND4: fast and accurate defocus estimation from electron micrographs. J. Struct. Biol. 192, 216\u2013221 (2015)","journal-title":"J. Struct. Biol."},{"key":"BFnature17964_CR47","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1006\/jsbi.1996.0030","volume":"116","author":"J Frank","year":"1996","unstructured":"Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol. 116, 190\u2013199 (1996)","journal-title":"J. Struct. Biol."},{"key":"BFnature17964_CR48","doi-asserted-by":"crossref","first-page":"e06980","DOI":"10.7554\/eLife.06980","volume":"4","author":"T Grant","year":"2015","unstructured":"Grant, T. & Grigorieff, N. Measuring the optimal exposure for single particle cryo-EM using a 2.6 \u00c5 reconstruction of rotavirus VP6. eLife 4, e06980 (2015)","journal-title":"eLife"},{"key":"BFnature17964_CR49","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.jsb.2012.09.006","volume":"180","author":"SHW Scheres","year":"2012","unstructured":"Scheres, S. H. W. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519\u2013530 (2012)","journal-title":"J. Struct. Biol."},{"key":"BFnature17964_CR50","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1038\/nmeth.2115","volume":"9","author":"SHW Scheres","year":"2012","unstructured":"Scheres, S. H. W. & Chen, S. Prevention of overfitting in cryo-EM structure determination. Nature Methods 9, 853\u2013854 (2012)","journal-title":"Nature Methods"},{"key":"BFnature17964_CR51","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1038\/nmeth.2727","volume":"11","author":"A Kucukelbir","year":"2014","unstructured":"Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nature Methods 11, 63\u201365 (2014)","journal-title":"Nature Methods"},{"key":"BFnature17964_CR52","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1016\/j.jsb.2006.07.003","volume":"157","author":"M Hohn","year":"2007","unstructured":"Hohn, M. et al. SPARX, a new environment for cryo-EM image processing. J. Struct. Biol. 157, 47\u201355 (2007)","journal-title":"J. Struct. Biol."},{"key":"BFnature17964_CR53","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1016\/j.jsb.2006.05.009","volume":"157","author":"G Tang","year":"2007","unstructured":"Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38\u201346 (2007)","journal-title":"J. Struct. Biol."},{"key":"BFnature17964_CR54","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","volume":"25","author":"EF Pettersen","year":"2004","unstructured":"Pettersen, E. F. et al. UCSF Chimera\u2014a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605\u20131612 (2004)","journal-title":"J. Comput. Chem."},{"key":"BFnature17964_CR55","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 66, 486\u2013501 (2010)","journal-title":"Acta Crystallogr. D"},{"key":"BFnature17964_CR56","doi-asserted-by":"crossref","first-page":"1074","DOI":"10.1107\/S0907444909029436","volume":"65","author":"NW Moriarty","year":"2009","unstructured":"Moriarty, N. W., Grosse-Kunstleve, R. W. & Adams, P. D. electronic Ligand Builder and Optimization Workbench (eLBOW): a tool for ligand coordinate and restraint generation. Acta Crystallogr. D 65, 1074\u20131080 (2009)","journal-title":"Acta Crystallogr. D"},{"key":"BFnature17964_CR57","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 66, 213\u2013221 (2010)","journal-title":"Acta Crystallogr. D"},{"key":"BFnature17964_CR58","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1007\/BF00355047","volume":"10","author":"DMF van Aalten","year":"1996","unstructured":"van Aalten, D. M. F. et al. PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules. J. Comput. Aided Mol. Des. 10, 255\u2013262 (1996)","journal-title":"J. Comput. Aided Mol. Des."},{"key":"BFnature17964_CR59","first-page":"43","volume":"4","author":"PV Afonine","year":"2013","unstructured":"Afonine, P. V., Headd, J. J., Terwilliger, T. C. & Adams, P. D. New tool: phenix. real_space_refine. Computational Crystallography Newsletter 4, 43\u201344 (2013)","journal-title":"Computational Crystallography Newsletter"},{"key":"BFnature17964_CR60","doi-asserted-by":"crossref","first-page":"1485","DOI":"10.1126\/science.1249410","volume":"343","author":"A Amunts","year":"2014","unstructured":"Amunts, A. et al. Structure of the yeast mitochondrial large ribosomal subunit. Science 343, 1485\u20131489 (2014)","journal-title":"Science"},{"key":"BFnature17964_CR61","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1107\/S0907444909042073","volume":"66","author":"VB Chen","year":"2010","unstructured":"Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D 66, 12\u201321 (2010)","journal-title":"Acta Crystallogr. D"}],"container-title":["Nature"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nature17964.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nature17964","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nature17964.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T13:51:57Z","timestamp":1684417917000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nature17964"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,5,18]]},"references-count":61,"journal-issue":{"issue":"7607","published-print":{"date-parts":[[2016,6]]}},"alternative-id":["BFnature17964"],"URL":"https:\/\/doi.org\/10.1038\/nature17964","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.726376549.793519358","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.726376549.793519222","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.726376549.793519022","asserted-by":"object"}]},"ISSN":["0028-0836","1476-4687"],"issn-type":[{"value":"0028-0836","type":"print"},{"value":"1476-4687","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,5,18]]},"assertion":[{"value":"9 December 2015","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"31 March 2016","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"18 May 2016","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing financial interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}