{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T07:54:33Z","timestamp":1791186873677,"version":"4.1.0"},"reference-count":51,"publisher":"Springer Science and Business Media LLC","issue":"9","license":[{"start":{"date-parts":[[2013,7,28]],"date-time":"2013-07-28T00:00:00Z","timestamp":1374969600000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Struct Mol Biol"],"published-print":{"date-parts":[[2013,9]]},"DOI":"10.1038\/nsmb.2628","type":"journal-article","created":{"date-parts":[[2013,7,28]],"date-time":"2013-07-28T14:51:15Z","timestamp":1375023075000},"page":"1062-1068","source":"Crossref","is-referenced-by-count":85,"title":["Structural basis for regulation of Arp2\/3 complex by GMF"],"prefix":"10.1038","volume":"20","author":[{"given":"Qing","family":"Luan","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brad J","family":"Nolen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2013,7,28]]},"reference":[{"key":"BFnsmb2628_CR1","doi-asserted-by":"publisher","first-page":"7","DOI":"10.1038\/nrm3492","volume":"14","author":"JD Rotty","year":"2013","unstructured":"Rotty, J.D., Wu, C. & Bear, J.E. New insights into the regulation and cellular functions of the ARP2\/3 complex. Nat. Rev. Mol. Cell Biol. 14, 7\u201312 (2013).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"BFnsmb2628_CR2","doi-asserted-by":"publisher","first-page":"713","DOI":"10.1038\/nrm2026","volume":"7","author":"ED Goley","year":"2006","unstructured":"Goley, E.D. & Welch, M.D. The ARP2\/3 complex: an actin nucleator comes of age. Nat. Rev. Mol. Cell Biol. 7, 713\u2013726 (2006).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"BFnsmb2628_CR3","doi-asserted-by":"publisher","first-page":"237","DOI":"10.1038\/nrm2867","volume":"11","author":"KG Campellone","year":"2010","unstructured":"Campellone, K.G. & Welch, M.D. A nucleator arms race: cellular control of actin assembly. Nat. Rev. Mol. Cell Biol. 11, 237\u2013251 (2010).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"BFnsmb2628_CR4","doi-asserted-by":"publisher","first-page":"451","DOI":"10.1146\/annurev.biophys.35.040405.101936","volume":"36","author":"TD Pollard","year":"2007","unstructured":"Pollard, T.D. Regulation of actin filament assembly by Arp2\/3 complex and formins. Annu. Rev. Biophys. Biomol. Struct. 36, 451\u2013477 (2007).","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"BFnsmb2628_CR5","doi-asserted-by":"publisher","first-page":"17039","DOI":"10.1074\/jbc.M111.219964","volume":"286","author":"SL Liu","year":"2011","unstructured":"Liu, S.L., Needham, K.M., May, J.R. & Nolen, B.J. Mechanism of a concentration-dependent switch between activation and inhibition of Arp2\/3 complex by coronin. J. Biol. Chem. 286, 17039\u201317046 (2011).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2628_CR6","doi-asserted-by":"publisher","first-page":"993","DOI":"10.1083\/jcb.200206113","volume":"159","author":"CL Humphries","year":"2002","unstructured":"Humphries, C.L. et al. Direct regulation of Arp2\/3 complex activity and function by the actin binding protein coronin. J. Cell Biol. 159, 993\u20131004 (2002).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2628_CR7","doi-asserted-by":"publisher","first-page":"399","DOI":"10.1083\/jcb.200212057","volume":"160","author":"RS Maul","year":"2003","unstructured":"Maul, R.S. et al. EPLIN regulates actin dynamics by cross-linking and stabilizing filaments. J. Cell Biol. 160, 399\u2013407 (2003).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2628_CR8","doi-asserted-by":"publisher","first-page":"1300","DOI":"10.1016\/S0960-9822(01)00395-5","volume":"11","author":"L Blanchoin","year":"2001","unstructured":"Blanchoin, L., Pollard, T.D. & Hitchcock-DeGregori, S.E. Inhibition of the Arp2\/3 complex-nucleated actin polymerization and branch formation by tropomyosin. Curr. Biol. 11, 1300\u20131304 (2001).","journal-title":"Curr. Biol."},{"key":"BFnsmb2628_CR9","doi-asserted-by":"publisher","first-page":"10382","DOI":"10.1073\/pnas.1206468109","volume":"109","author":"T Maritzen","year":"2012","unstructured":"Maritzen, T. et al. Gadkin negatively regulates cell spreading and motility via sequestration of the actin-nucleating ARP2\/3 complex. Proc. Natl. Acad. Sci. USA 109, 10382\u201310387 (2012).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2628_CR10","doi-asserted-by":"publisher","first-page":"259","DOI":"10.1038\/ncb1688","volume":"10","author":"DL Rocca","year":"2008","unstructured":"Rocca, D.L., Martin, S., Jenkins, E.L. & Hanley, J.G. Inhibition of Arp2\/3-mediated actin polymerization by PICK1 regulates neuronal morphology and AMPA receptor endocytosis. Nat. Cell Biol. 10, 259\u2013271 (2008).","journal-title":"Nat. Cell Biol."},{"key":"BFnsmb2628_CR11","doi-asserted-by":"publisher","first-page":"17937","DOI":"10.1074\/jbc.M208739200","volume":"278","author":"Y Yamakita","year":"2003","unstructured":"Yamakita, Y., Oosawa, F., Yamashiro, S. & Matsumura, F. Caldesmon inhibits Arp2\/3-mediated actin nucleation. J. Biol. Chem. 278, 17937\u201317944 (2003).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2628_CR12","doi-asserted-by":"publisher","first-page":"861","DOI":"10.1016\/j.cub.2010.03.026","volume":"20","author":"M Gandhi","year":"2010","unstructured":"Gandhi, M. et al. GMF is a cofilin homolog that binds Arp2\/3 complex to stimulate filament debranching and inhibit actin nucleation. Curr. Biol. 20, 861\u2013867 (2010).","journal-title":"Curr. Biol."},{"key":"BFnsmb2628_CR13","doi-asserted-by":"publisher","first-page":"E463","DOI":"10.1073\/pnas.1100125108","volume":"108","author":"SC Ti","year":"2011","unstructured":"Ti, S.C., Jurgenson, C.T., Nolen, B.J. & Pollard, T.D. Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2\/3 complex. Proc. Natl. Acad. Sci. USA 108, E463\u2013E471 (2011).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2628_CR14","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1002\/cm.20451","volume":"67","author":"K Nakano","year":"2010","unstructured":"Nakano, K., Kuwayama, H., Kawasaki, M., Numata, O. & Takaine, M. GMF is an evolutionarily developed Adf\/cofilin-super family protein involved in the Arp2\/3 complex-mediated organization of the actin cytoskeleton. Cytoskeleton (Hoboken) 67, 373\u2013382 (2010).","journal-title":"Cytoskeleton (Hoboken)"},{"key":"BFnsmb2628_CR15","doi-asserted-by":"publisher","first-page":"424","DOI":"10.1161\/01.RES.0000237662.23539.0b","volume":"99","author":"K Ikeda","year":"2006","unstructured":"Ikeda, K. et al. Glia maturation factor-\u03b3 is preferentially expressed in microvascular endothelial and inflammatory cells and modulates actin cytoskeleton reorganization. Circ. Res. 99, 424\u2013433 (2006).","journal-title":"Circ. Res."},{"key":"BFnsmb2628_CR16","doi-asserted-by":"publisher","first-page":"471","DOI":"10.1002\/cm.20530","volume":"68","author":"M Poukkula","year":"2011","unstructured":"Poukkula, M., Kremneva, E., Serlachius, M. & Lappalainen, P. Actin-depolymerizing factor homology domain: a conserved fold performing diverse roles in cytoskeletal dynamics. Cytoskeleton (Hoboken) 68, 471\u2013490 (2011).","journal-title":"Cytoskeleton (Hoboken)"},{"key":"BFnsmb2628_CR17","doi-asserted-by":"publisher","first-page":"661","DOI":"10.1146\/annurev-biochem-060910-094416","volume":"81","author":"OL Mooren","year":"2012","unstructured":"Mooren, O.L., Galletta, B.J. & Cooper, J.A. Roles for actin assembly in endocytosis. Annu. Rev. Biochem. 81, 661\u2013686 (2012).","journal-title":"Annu. Rev. Biochem."},{"key":"BFnsmb2628_CR18","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1016\/j.cub.2013.04.058","volume":"23","author":"C Ydenberg","year":"2013","unstructured":"Ydenberg, C. et al. GMF severs actin-Arp2\/3 complex branch junctions by a cofilin-like mechanism. Curr. Biol. 23, 1\u20139 (2013).","journal-title":"Curr. Biol."},{"key":"BFnsmb2628_CR19","doi-asserted-by":"publisher","first-page":"15627","DOI":"10.1073\/pnas.0407149101","volume":"101","author":"BJ Nolen","year":"2004","unstructured":"Nolen, B.J., Littlefield, R.S. & Pollard, T.D. Crystal structures of actin-related protein 2\/3 complex with bound ATP or ADP. Proc. Natl. Acad. Sci. USA 101, 15627\u201315632 (2004).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2628_CR20","doi-asserted-by":"publisher","first-page":"51","DOI":"10.1083\/jcb.200803100","volume":"182","author":"VO Paavilainen","year":"2008","unstructured":"Paavilainen, V.O., Oksanen, E., Goldman, A. & Lappalainen, P. Structure of the actin-depolymerizing factor homology domain in complex with actin. J. Cell Biol. 182, 51\u201359 (2008).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2628_CR21","doi-asserted-by":"publisher","first-page":"20568","DOI":"10.1073\/pnas.1110109108","volume":"108","author":"VE Galkin","year":"2011","unstructured":"Galkin, V.E. et al. Remodeling of actin filaments by ADF\/cofilin proteins. Proc. Natl. Acad. Sci. USA 108, 20568\u201320572 (2011).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2628_CR22","doi-asserted-by":"publisher","first-page":"2384","DOI":"10.1002\/pro.248","volume":"18","author":"AK Goroncy","year":"2009","unstructured":"Goroncy, A.K. et al. NMR solution structures of actin depolymerizing factor homology domains. Protein Sci. 18, 2384\u20132392 (2009).","journal-title":"Protein Sci."},{"key":"BFnsmb2628_CR23","doi-asserted-by":"publisher","first-page":"5520","DOI":"10.1093\/emboj\/16.18.5520","volume":"16","author":"P Lappalainen","year":"1997","unstructured":"Lappalainen, P., Fedorov, E.V., Fedorov, A.A., Almo, S.C. & Drubin, D.G. Essential functions and actin-binding surfaces of yeast cofilin revealed by systematic mutagenesis. EMBO J. 16, 5520\u20135530 (1997).","journal-title":"EMBO J."},{"key":"BFnsmb2628_CR24","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1146\/annurev.cellbio.15.1.185","volume":"15","author":"JR Bamburg","year":"1999","unstructured":"Bamburg, J.R. Proteins of the ADF\/cofilin family: essential regulators of actin dynamics. Annu. Rev. Cell Dev. Biol. 15, 185\u2013230 (1999).","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"BFnsmb2628_CR25","doi-asserted-by":"publisher","first-page":"572","DOI":"10.1016\/j.tibs.2004.09.004","volume":"29","author":"R Dominguez","year":"2004","unstructured":"Dominguez, R. Actin-binding proteins: a unifying hypothesis. Trends Biochem. Sci. 29, 572\u2013578 (2004).","journal-title":"Trends Biochem. Sci."},{"key":"BFnsmb2628_CR26","doi-asserted-by":"publisher","first-page":"449","DOI":"10.1016\/j.molcel.2007.04.017","volume":"26","author":"BJ Nolen","year":"2007","unstructured":"Nolen, B.J. & Pollard, T.D. Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2\/3 complex. Mol. Cell 26, 449\u2013457 (2007).","journal-title":"Mol. Cell"},{"key":"BFnsmb2628_CR27","doi-asserted-by":"publisher","first-page":"826","DOI":"10.1038\/ncb1443","volume":"8","author":"AC Martin","year":"2006","unstructured":"Martin, A.C., Welch, M.D. & Drubin, D.G. Arp2\/3 ATP hydrolysis-catalysed branch dissociation is critical for endocytic force generation. Nat. Cell Biol. 8, 826\u2013833 (2006).","journal-title":"Nat. Cell Biol."},{"key":"BFnsmb2628_CR28","doi-asserted-by":"publisher","first-page":"619","DOI":"10.1083\/jcb.201211069","volume":"200","author":"E Ingerman","year":"2013","unstructured":"Ingerman, E., Hsiao, J.Y. & Mullins, R.D. Arp2\/3 complex ATP hydrolysis promotes lamellipodial actin network disassembly but is dispensable for assembly. J. Cell Biol. 200, 619\u2013633 (2013).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2628_CR29","doi-asserted-by":"publisher","first-page":"708","DOI":"10.1126\/science.1059700","volume":"293","author":"LR Otterbein","year":"2001","unstructured":"Otterbein, L.R., Graceffa, P. & Dominguez, R. The crystal structure of uncomplexed actin in the ADP state. Science 293, 708\u2013711 (2001).","journal-title":"Science"},{"key":"BFnsmb2628_CR30","doi-asserted-by":"crossref","unstructured":"Hetrick, B., Han, M.S., Helgeson, L.A. & Nolen, B.J. Small molecules CK-666 and CK-869 inhibit Arp2\/3 complex by blocking an activating conformational change. Chem. Biol. 701\u2013712 (2013).","DOI":"10.1016\/j.chembiol.2013.03.019"},{"key":"BFnsmb2628_CR31","doi-asserted-by":"publisher","first-page":"E472","DOI":"10.1073\/pnas.1100236108","volume":"108","author":"SB Padrick","year":"2011","unstructured":"Padrick, S.B., Doolittle, L.K., Brautigam, C.A., King, D.S. & Rosen, M.K. Arp2\/3 complex is bound and activated by two WASP proteins. Proc. Natl. Acad. Sci. USA 108, E472\u2013E479 (2011).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2628_CR32","doi-asserted-by":"publisher","first-page":"591","DOI":"10.1038\/nsb952","volume":"10","author":"SC Panchal","year":"2003","unstructured":"Panchal, S.C., Kaiser, D.A., Torres, E., Pollard, T.D. & Rosen, M.K. A conserved amphipathic helix in WASP\/Scar proteins is essential for activation of Arp2\/3 complex. Nat. Struct. Biol. 10, 591\u2013598 (2003).","journal-title":"Nat. Struct. Biol."},{"key":"BFnsmb2628_CR33","doi-asserted-by":"publisher","first-page":"16644","DOI":"10.1073\/pnas.0507021102","volume":"102","author":"D Chereau","year":"2005","unstructured":"Chereau, D. et al. Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 and the implications for filament assembly. Proc. Natl. Acad. Sci. USA 102, 16644\u201316649 (2005).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2628_CR34","doi-asserted-by":"publisher","first-page":"3599","DOI":"10.1038\/sj.emboj.7600372","volume":"23","author":"E Irobi","year":"2004","unstructured":"Irobi, E. et al. Structural basis of actin sequestration by thymosin-\u03b24: implications for WH2 proteins. EMBO J. 23, 3599\u20133608 (2004).","journal-title":"EMBO J."},{"key":"BFnsmb2628_CR35","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1038\/35050590","volume":"3","author":"JB Marchand","year":"2001","unstructured":"Marchand, J.B., Kaiser, D.A., Pollard, T.D. & Higgs, H.N. Interaction of WASP\/Scar proteins with actin and vertebrate Arp2\/3 complex. Nat. Cell Biol. 3, 76\u201382 (2001).","journal-title":"Nat. Cell Biol."},{"key":"BFnsmb2628_CR36","doi-asserted-by":"publisher","first-page":"8481","DOI":"10.1074\/jbc.M109.054957","volume":"285","author":"HI Balcer","year":"2010","unstructured":"Balcer, H.I., Daugherty-Clarke, K. & Goode, B.L. The p40\/ARPC1 subunit of Arp2\/3 complex performs multiple essential roles in WASp-regulated actin nucleation. J. Biol. Chem. 285, 8481\u20138491 (2010).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2628_CR37","doi-asserted-by":"publisher","first-page":"537","DOI":"10.1016\/j.cub.2009.02.060","volume":"19","author":"C Chan","year":"2009","unstructured":"Chan, C., Beltzner, C.C. & Pollard, T.D. Cofilin dissociates Arp2\/3 complex and branches from actin filaments. Curr. Biol. 19, 537\u2013545 (2009).","journal-title":"Curr. Biol."},{"key":"BFnsmb2628_CR38","doi-asserted-by":"publisher","first-page":"887","DOI":"10.1083\/jcb.200709092","volume":"180","author":"I Rouiller","year":"2008","unstructured":"Rouiller, I. et al. The structural basis of actin filament branching by the Arp2\/3 complex. J. Cell Biol. 180, 887\u2013895 (2008).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2628_CR39","doi-asserted-by":"publisher","first-page":"695","DOI":"10.1016\/j.str.2008.02.013","volume":"16","author":"M Boczkowska","year":"2008","unstructured":"Boczkowska, M. et al. X-Ray scattering study of activated Arp2\/3 complex with bound actin-WCA. Structure 16, 695\u2013704 (2008).","journal-title":"Structure"},{"key":"BFnsmb2628_CR40","doi-asserted-by":"publisher","first-page":"1270","DOI":"10.1016\/S0960-9822(02)01035-7","volume":"12","author":"AM Weaver","year":"2002","unstructured":"Weaver, A.M. et al. Interaction of cortactin and N-WASp with Arp2\/3 complex. Curr. Biol. 12, 1270\u20131278 (2002).","journal-title":"Curr. Biol."},{"key":"BFnsmb2628_CR41","doi-asserted-by":"publisher","first-page":"26086","DOI":"10.1074\/jbc.M301997200","volume":"278","author":"T Uruno","year":"2003","unstructured":"Uruno, T., Liu, J., Li, Y., Smith, N. & Zhan, X. Sequential interaction of actin-related proteins 2 and 3 (Arp2\/3) complex with neural Wiscott-Aldrich syndrome protein (N-WASP) and cortactin during branched actin filament network formation. J. Biol. Chem. 278, 26086\u201326093 (2003).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2628_CR42","doi-asserted-by":"publisher","first-page":"3519","DOI":"10.1529\/biophysj.106.080937","volume":"91","author":"RE Mahaffy","year":"2006","unstructured":"Mahaffy, R.E. & Pollard, T.D. Kinetics of the formation and dissociation of actin filament branches mediated by Arp2\/3 complex. Biophys. J. 91, 3519\u20133528 (2006).","journal-title":"Biophys. J."},{"key":"BFnsmb2628_CR43","doi-asserted-by":"publisher","first-page":"828","DOI":"10.1016\/j.cell.2008.06.054","volume":"134","author":"L Cai","year":"2008","unstructured":"Cai, L., Makhov, A.M., Schafer, D.A. & Bear, J.E. Coronin 1B antagonizes cortactin and remodels Arp2\/3-containing actin branches in lamellipodia. Cell 134, 828\u2013842 (2008).","journal-title":"Cell"},{"key":"BFnsmb2628_CR44","doi-asserted-by":"publisher","first-page":"370","DOI":"10.1016\/S0960-9822(01)00098-7","volume":"11","author":"AM Weaver","year":"2001","unstructured":"Weaver, A.M. et al. Cortactin promotes and stabilizes Arp2\/3-induced actin filament network formation. Curr. Biol. 11, 370\u2013374 (2001).","journal-title":"Curr. Biol."},{"key":"BFnsmb2628_CR45","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1002\/cm.970020102","volume":"2","author":"BW Bernstein","year":"1982","unstructured":"Bernstein, B.W. & Bamburg, J.R. Tropomyosin binding to F-actin protects the F-actin from disassembly by brain actin-depolymerizing factor (ADF). Cell Motil. 2, 1\u20138 (1982).","journal-title":"Cell Motil."},{"key":"BFnsmb2628_CR46","doi-asserted-by":"publisher","first-page":"34172","DOI":"10.1074\/jbc.M303689200","volume":"278","author":"P Graceffa","year":"2003","unstructured":"Graceffa, P. & Dominguez, R. Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics. J. Biol. Chem. 278, 34172\u201334180 (2003).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2628_CR47","doi-asserted-by":"publisher","first-page":"W529","DOI":"10.1093\/nar\/gkq399","volume":"38","author":"H Ashkenazy","year":"2010","unstructured":"Ashkenazy, H., Erez, E., Martz, E., Pupko, T. & Ben-Tal, N. ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res. 38, W529\u2013W533 (2010).","journal-title":"Nucleic Acids Res."},{"key":"BFnsmb2628_CR48","doi-asserted-by":"publisher","first-page":"26490","DOI":"10.1074\/jbc.M802607200","volume":"283","author":"BJ Nolen","year":"2008","unstructured":"Nolen, B.J. & Pollard, T.D. Structure and biochemical properties of fission yeast ARP2\/3 complex lacking the ARP2 subunit. J. Biol. Chem. 283, 26490\u201326498 (2008).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2628_CR49","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1016\/S0076-6879(97)76066-X","volume":"276","author":"Z Otwinowski","year":"1997","unstructured":"Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data dollected in oscillation mode. Methods Enzymol. 276, 307\u2013326 (1997).","journal-title":"Methods Enzymol."},{"key":"BFnsmb2628_CR50","doi-asserted-by":"publisher","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":"BFnsmb2628_CR51","doi-asserted-by":"publisher","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."}],"container-title":["Nature Structural & Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2628.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2628","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2628.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2024,5,15]],"date-time":"2024-05-15T10:25:54Z","timestamp":1715768754000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nsmb.2628"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,7,28]]},"references-count":51,"journal-issue":{"issue":"9","published-print":{"date-parts":[[2013,9]]}},"alternative-id":["BFnsmb2628"],"URL":"https:\/\/doi.org\/10.1038\/nsmb.2628","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.718050300.793484581","asserted-by":"object"},{"id-type":"doi","id":"10.3410\/f.718050300.793481308","asserted-by":"object"}]},"ISSN":["1545-9993","1545-9985"],"issn-type":[{"value":"1545-9993","type":"print"},{"value":"1545-9985","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,7,28]]}}}