{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T21:16:05Z","timestamp":1793049365979,"version":"4.5.0"},"reference-count":68,"publisher":"Elsevier BV","issue":"23","license":[{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,12,7]],"date-time":"2024-12-07T00:00:00Z","timestamp":1733529600000},"content-version":"vor","delay-in-days":372,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"},{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2023,12,1]],"date-time":"2023-12-01T00:00:00Z","timestamp":1701388800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Molecular Cell"],"published-print":{"date-parts":[[2023,12]]},"DOI":"10.1016\/j.molcel.2023.10.038","type":"journal-article","created":{"date-parts":[[2023,11,22]],"date-time":"2023-11-22T10:33:49Z","timestamp":1700649229000},"page":"4398-4412.e4","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":24,"title":["Structural insights into the assembly and mechanism of mpox virus DNA polymerase complex F8-A22-E4-H5"],"prefix":"10.1016","volume":"83","author":[{"given":"Xiaohan","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Liangwen","family":"Ma","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ningning","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3067-9993","authenticated-orcid":false,"given":"Ning","family":"Gao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.molcel.2023.10.038_bib1","series-title":"Fields Virologya: DNA Viruses","first-page":"573","article-title":"Poxviridae: the viruses and their replication","author":"Moss","year":"2021"},{"key":"10.1016\/j.molcel.2023.10.038_bib2","doi-asserted-by":"crossref","first-page":"2031","DOI":"10.1091\/mbc.12.7.2031","article-title":"Vaccinia virus DNA replication occurs in endoplasmic reticulum-enclosed cytoplasmic mini-nuclei","volume":"12","author":"Tolonen","year":"2001","journal-title":"Mol. Biol. Cell"},{"key":"10.1016\/j.molcel.2023.10.038_bib3","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1146\/annurev-virology-091919-104752","article-title":"The life cycle of the vaccinia virus genome","volume":"9","author":"Greseth","year":"2022","journal-title":"Annu. Rev. Virol."},{"key":"10.1016\/j.molcel.2023.10.038_bib4","doi-asserted-by":"crossref","first-page":"a010199","DOI":"10.1101\/cshperspect.a010199","article-title":"Poxvirus DNA replication","volume":"5","author":"Moss","year":"2013","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"10.1016\/j.molcel.2023.10.038_bib5","doi-asserted-by":"crossref","first-page":"6312","DOI":"10.1128\/JVI.00445-15","article-title":"Genetic confirmation that the H5 protein is required for vaccinia virus DNA replication","volume":"89","author":"Boyle","year":"2015","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.molcel.2023.10.038_bib6","doi-asserted-by":"crossref","first-page":"7812","DOI":"10.1016\/S0021-9258(18)36019-8","article-title":"Purification and properties of the deoxyribonucleic acid polymerase induced by vaccinia virus","volume":"254","author":"Challberg","year":"1979","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.molcel.2023.10.038_bib7","doi-asserted-by":"crossref","first-page":"4879","DOI":"10.1073\/pnas.080078197","article-title":"Genome-wide analysis of vaccinia virus protein-protein interactions","volume":"97","author":"McCraith","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.molcel.2023.10.038_bib8","doi-asserted-by":"crossref","first-page":"3439","DOI":"10.1074\/jbc.M511239200","article-title":"Vaccinia virus uracil DNA glycosylase interacts with the A20 protein to form a heterodimeric processivity factor for the viral DNA polymerase","volume":"281","author":"Stanitsa","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.molcel.2023.10.038_bib9","doi-asserted-by":"crossref","first-page":"4604","DOI":"10.1128\/JVI.00044-16","article-title":"Domain organization of vaccinia virus helicase-primase D5","volume":"90","author":"Hutin","year":"2016","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.molcel.2023.10.038_bib10","doi-asserted-by":"crossref","first-page":"2917","DOI":"10.1128\/JVI.72.4.2917-2926.1998","article-title":"Characterization of the single-stranded DNA binding protein encoded by the vaccinia virus I3 gene","volume":"72","author":"Rochester","year":"1998","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.molcel.2023.10.038_bib11","doi-asserted-by":"crossref","first-page":"31190","DOI":"10.1016\/S0021-9258(18)47408-X","article-title":"Vaccinia virus DNA polymerase. In\u00a0vitro analysis of parameters affecting processivity","volume":"269","author":"McDonald","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.molcel.2023.10.038_bib12","doi-asserted-by":"crossref","first-page":"12298","DOI":"10.1128\/JVI.75.24.12298-12307.2001","article-title":"The A20R protein is a stoichiometric component of the processive form of vaccinia virus DNA polymerase","volume":"75","author":"Klemperer","year":"2001","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.molcel.2023.10.038_bib13","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1016\/j.virusres.2017.01.027","article-title":"The vaccinia virus DNA polymerase and its processivity factor","volume":"234","author":"Czarnecki","year":"2017","journal-title":"Virus Res."},{"key":"10.1016\/j.molcel.2023.10.038_bib14","doi-asserted-by":"crossref","first-page":"2503","DOI":"10.1128\/jvi.67.5.2503-2512.1993","article-title":"A poxvirus-encoded uracil DNA glycosylase is essential for virus viability","volume":"67","author":"Stuart","year":"1993","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.molcel.2023.10.038_bib15","doi-asserted-by":"crossref","first-page":"1667","DOI":"10.1002\/pro.2554","article-title":"Uracil-DNA glycosylases-Structural and functional perspectives on an essential family of DNA repair enzymes","volume":"23","author":"Schormann","year":"2014","journal-title":"Protein Sci."},{"key":"10.1016\/j.molcel.2023.10.038_bib16","doi-asserted-by":"crossref","first-page":"24702","DOI":"10.1074\/jbc.M111.222216","article-title":"Evaluation of the role of the vaccinia virus uracil DNA glycosylase and A20 proteins as intrinsic components of the DNA polymerase holoenzyme","volume":"286","author":"Boyle","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.molcel.2023.10.038_bib17","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1128\/JVI.77.1.159-166.2003","article-title":"Vaccinia virus uracil DNA glycosylase has an essential role in DNA synthesis that is independent of its glycosylase activity: catalytic site mutations reduce virulence but not virus replication in cultured cells","volume":"77","author":"De Silva","year":"2003","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.molcel.2023.10.038_bib18","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/j.virol.2010.01.020","article-title":"Vaccinia H5 is a multifunctional protein involved in viral DNA replication, postreplicative gene transcription, and virion morphogenesis","volume":"401","author":"D'Costa","year":"2010","journal-title":"Virology"},{"key":"10.1016\/j.molcel.2023.10.038_bib19","doi-asserted-by":"crossref","first-page":"6796","DOI":"10.1128\/jvi.70.10.6796-6802.1996","article-title":"The vaccinia virus H5R gene encodes late gene transcription factor 4: purification, cloning, and overexpression","volume":"70","author":"Kovacs","year":"1996","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.molcel.2023.10.038_bib20","doi-asserted-by":"crossref","first-page":"eadg2331","DOI":"10.1126\/sciadv.adg2331","article-title":"Structural basis for the assembly of the DNA polymerase holoenzyme from a monkeypox virus variant","volume":"9","author":"Li","year":"2023","journal-title":"Sci. Adv."},{"key":"10.1016\/j.molcel.2023.10.038_bib21","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1126\/science.ade6360","article-title":"Structure of monkeypox virus DNA polymerase holoenzyme","volume":"379","author":"Peng","year":"2023","journal-title":"Science"},{"key":"10.1016\/j.molcel.2023.10.038_bib22","doi-asserted-by":"crossref","first-page":"479","DOI":"10.1038\/s41422-023-00796-1","article-title":"Cryo-EM structures of human monkeypox viral replication complexes with and without DNA duplex","volume":"33","author":"Xu","year":"2023","journal-title":"Cell Res."},{"key":"10.1016\/j.molcel.2023.10.038_bib23","doi-asserted-by":"crossref","first-page":"1679","DOI":"10.1128\/JVI.01533-12","article-title":"Low-resolution structure of vaccinia virus DNA replication machinery","volume":"87","author":"S\u00e8le","year":"2013","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.molcel.2023.10.038_bib24","doi-asserted-by":"crossref","first-page":"11470","DOI":"10.1074\/jbc.M112.442012","article-title":"Biochemical and biophysical properties of a putative hub protein expressed by vaccinia virus","volume":"288","author":"Kay","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.molcel.2023.10.038_bib25","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1038\/s41467-017-01542-z","article-title":"The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding","volume":"8","author":"Tarbouriech","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.molcel.2023.10.038_bib26","doi-asserted-by":"crossref","first-page":"167009","DOI":"10.1016\/j.jmb.2021.167009","article-title":"Solution structure of the C-terminal domain of A20, the missing brick for the characterization of the interface between vaccinia virus DNA polymerase and its processivity factor","volume":"433","author":"Bersch","year":"2021","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.molcel.2023.10.038_bib27","doi-asserted-by":"crossref","first-page":"17923","DOI":"10.1074\/jbc.M115.648352","article-title":"Crystal structure of the vaccinia virus uracil-DNA glycosylase in complex with DNA","volume":"290","author":"Burmeister","year":"2015","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.molcel.2023.10.038_bib28","doi-asserted-by":"crossref","first-page":"e1003978","DOI":"10.1371\/journal.ppat.1003978","article-title":"Crystal structure of the vaccinia virus DNA polymerase holoenzyme Subunit D4 in complex with the A20 N-terminal domain","volume":"10","author":"Contesto-Richefeu","year":"2014","journal-title":"PLoS Pathog."},{"key":"10.1016\/j.molcel.2023.10.038_bib29","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1038\/nsmb.1663","article-title":"Structural basis of high-fidelity DNA synthesis by yeast DNA polymerase delta","volume":"16","author":"Swan","year":"2009","journal-title":"Nat. Struct. Mol. Biol."},{"key":"10.1016\/j.molcel.2023.10.038_bib30","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/S0065-3233(04)71011-6","article-title":"Structure and mechanism of DNA polymerases","volume":"71","author":"Rothwell","year":"2005","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.molcel.2023.10.038_bib31","doi-asserted-by":"crossref","first-page":"17395","DOI":"10.1074\/jbc.274.25.17395","article-title":"DNA polymerases: structural diversity and common mechanisms","volume":"274","author":"Steitz","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.molcel.2023.10.038_bib32","doi-asserted-by":"crossref","first-page":"7514","DOI":"10.1093\/emboj\/17.24.7514","article-title":"Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation","volume":"17","author":"Li","year":"1998","journal-title":"EMBO J."},{"key":"10.1016\/j.molcel.2023.10.038_bib33","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1038\/34593","article-title":"Crystal structure of a bacteriophage T7 DNA replication complex at 2.2\u00a0\u00c5 resolution","volume":"391","author":"Doubli\u00e9","year":"1998","journal-title":"Nature"},{"key":"10.1016\/j.molcel.2023.10.038_bib34","doi-asserted-by":"crossref","first-page":"R31","DOI":"10.1016\/S0969-2126(99)80017-3","article-title":"An open and closed case for all polymerases","volume":"7","author":"Doubli\u00e9","year":"1999","journal-title":"Structure"},{"key":"10.1016\/j.molcel.2023.10.038_bib35","doi-asserted-by":"crossref","first-page":"1669","DOI":"10.1126\/science.282.5394.1669","article-title":"Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance","volume":"282","author":"Huang","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.molcel.2023.10.038_bib36","doi-asserted-by":"crossref","first-page":"14317","DOI":"10.1021\/bi048422z","article-title":"DNA polymerase fidelity: kinetics, structure, and checkpoints","volume":"43","author":"Joyce","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.molcel.2023.10.038_bib37","doi-asserted-by":"crossref","first-page":"20","DOI":"10.3389\/fmolb.2016.00020","article-title":"DNA polymerase conformational dynamics and the role of fidelity-conferring residues: insights from computational simulations","volume":"3","author":"Meli","year":"2016","journal-title":"Front. Mol. Biosci."},{"key":"10.1016\/j.molcel.2023.10.038_bib38","doi-asserted-by":"crossref","first-page":"2113","DOI":"10.1002\/pro.3058","article-title":"Poxvirus uracil-DNA glycosylase-an unusual member of the family I uracil-DNA glycosylases","volume":"25","author":"Schormann","year":"2016","journal-title":"Protein Sci."},{"key":"10.1016\/j.molcel.2023.10.038_bib39","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1016\/S0921-8777(00)00025-2","article-title":"Structure and function in the uracil-DNA glycosylase superfamily","volume":"460","author":"Pearl","year":"2000","journal-title":"Mutat. Res."},{"key":"10.1016\/j.molcel.2023.10.038_bib40","doi-asserted-by":"crossref","first-page":"5214","DOI":"10.1093\/emboj\/17.17.5214","article-title":"Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA","volume":"17","author":"Parikh","year":"1998","journal-title":"EMBO J."},{"key":"10.1016\/j.molcel.2023.10.038_bib41","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1038\/nature06131","article-title":"Enzymatic capture of an extrahelical thymine in the search for uracil in DNA","volume":"449","author":"Parker","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.molcel.2023.10.038_bib42","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/S0921-8777(00)00026-4","article-title":"Lessons learned from structural results on uracil-DNA glycosylase","volume":"460","author":"Parikh","year":"2000","journal-title":"Mutat. Res."},{"key":"10.1016\/j.molcel.2023.10.038_bib43","doi-asserted-by":"crossref","first-page":"8291","DOI":"10.1093\/nar\/gkr564","article-title":"Computational analysis of DNA replicases in double-stranded DNA viruses: relationship with the genome size","volume":"39","author":"Kazlauskas","year":"2011","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.molcel.2023.10.038_bib44","doi-asserted-by":"crossref","first-page":"2058","DOI":"10.3390\/genes13112058","article-title":"From processivity to genome maintenance: the many roles of sliding clamps","volume":"13","author":"Mulye","year":"2022","journal-title":"Genes (Basel)"},{"key":"10.1016\/j.molcel.2023.10.038_bib45","doi-asserted-by":"crossref","first-page":"30344","DOI":"10.1073\/pnas.2017637117","article-title":"Structure of eukaryotic DNA polymerase \u03b4 bound to the PCNA clamp while encircling DNA","volume":"117","author":"Zheng","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.molcel.2023.10.038_bib46","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/0092-8674(92)90445-I","article-title":"Three-dimensional structure of the \u03b2-subunit of E. -coli DNA polymerase III holoenzyme: a sliding DNA clamp","volume":"69","author":"Kong","year":"1992","journal-title":"Cell"},{"key":"10.1016\/j.molcel.2023.10.038_bib47","series-title":"The Enzymes","first-page":"133","article-title":"Herpesvirus DNA polymerase: structures, functions, and mechanisms","author":"Coen","year":"2021"},{"key":"10.1016\/j.molcel.2023.10.038_bib48","doi-asserted-by":"crossref","first-page":"6154","DOI":"10.1074\/jbc.M708691200","article-title":"The positively charged surface of herpes simplex virus UL42 mediates DNA binding","volume":"283","author":"Komazin-Meredith","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.molcel.2023.10.038_bib49","doi-asserted-by":"crossref","first-page":"4779","DOI":"10.1093\/nar\/gkm506","article-title":"Binding parameters and thermodynamics of the interaction of the human cytomegalovirus DNA polymerase accessory protein, UL44, with DNA: implications for the processivity mechanism","volume":"35","author":"Loregian","year":"2007","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.molcel.2023.10.038_bib50","doi-asserted-by":"crossref","first-page":"198394","DOI":"10.1016\/j.virusres.2021.198394","article-title":"Herpesvirus DNA polymerase processivity factors: not just for DNA synthesis","volume":"298","author":"Cohan","year":"2021","journal-title":"Virus Res."},{"key":"10.1016\/j.molcel.2023.10.038_bib51","series-title":"The Enzymes","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1016\/bs.enz.2016.03.003","article-title":"The many roles of PCNA in eukaryotic DNA replication","author":"Boehm","year":"2016"},{"key":"10.1016\/j.molcel.2023.10.038_bib52","doi-asserted-by":"crossref","first-page":"10908","DOI":"10.1073\/pnas.1514809112","article-title":"Mapping vaccinia virus DNA replication origins at nucleotide level by deep sequencing","volume":"112","author":"Senkevich","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.molcel.2023.10.038_bib53","doi-asserted-by":"crossref","first-page":"18724","DOI":"10.1073\/pnas.0709276104","article-title":"Poxvirus DNA primase","volume":"104","author":"De Silva","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.molcel.2023.10.038_bib54","doi-asserted-by":"crossref","first-page":"232","DOI":"10.1006\/viro.2002.1721","article-title":"Mapping interaction sites of the A20R protein component of the vaccinia virus DNA replication complex","volume":"303","author":"Ishii","year":"2002","journal-title":"Virology"},{"key":"10.1016\/j.molcel.2023.10.038_bib55","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.chom.2007.03.007","article-title":"Poxviral b1 kinase overcomes barrier to autointegration factor, a host Defense against virus replication","volume":"1","author":"Wiebe","year":"2007","journal-title":"Cell Host Microbe"},{"key":"10.1016\/j.molcel.2023.10.038_bib56","doi-asserted-by":"crossref","first-page":"1819","DOI":"10.1128\/jvi.69.3.1819-1826.1995","article-title":"Vaccinia virus gene H5r encodes a protein that is phosphorylated by the multisubstrate vaccinia virus B1r protein kinase","volume":"69","author":"Beaud","year":"1995","journal-title":"J.\u00a0Virol."},{"key":"10.1016\/j.molcel.2023.10.038_bib57","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.jsb.2012.09.006","article-title":"RELION: implementation of a Bayesian approach to cryo-EM structure determination","volume":"180","author":"Scheres","year":"2012","journal-title":"J.\u00a0Struct. Biol."},{"key":"10.1016\/j.molcel.2023.10.038_bib58","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1038\/nmeth.4169","article-title":"cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination","volume":"14","author":"Punjani","year":"2017","journal-title":"Nat. Methods"},{"key":"10.1016\/j.molcel.2023.10.038_bib59","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/nmeth.4193","article-title":"MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy","volume":"14","author":"Zheng","year":"2017","journal-title":"Nat. Methods"},{"key":"10.1016\/j.molcel.2023.10.038_bib60","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.jsb.2015.08.008","article-title":"CTFFIND4: fast and accurate defocus estimation from electron micrographs","volume":"192","author":"Rohou","year":"2015","journal-title":"J.\u00a0Struct. Biol."},{"key":"10.1016\/j.molcel.2023.10.038_bib61","doi-asserted-by":"crossref","first-page":"1153","DOI":"10.1038\/s41592-019-0575-8","article-title":"Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs","volume":"16","author":"Bepler","year":"2019","journal-title":"Nat. Methods"},{"key":"10.1016\/j.molcel.2023.10.038_bib62","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera--a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.molcel.2023.10.038_bib63","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1002\/pro.3943","article-title":"UCSF ChimeraX: structure visualization for researchers, educators, and developers","volume":"30","author":"Pettersen","year":"2021","journal-title":"Protein Sci."},{"key":"10.1016\/j.molcel.2023.10.038_bib64","doi-asserted-by":"crossref","first-page":"583","DOI":"10.1038\/s41586-021-03819-2","article-title":"Highly accurate protein structure prediction with AlphaFold","volume":"596","author":"Jumper","year":"2021","journal-title":"Nature"},{"key":"10.1016\/j.molcel.2023.10.038_bib65","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1107\/S0907444910007493","article-title":"Features and development of Coot","volume":"66","author":"Emsley","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.molcel.2023.10.038_bib66","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1107\/S0907444909052925","article-title":"PHENIX: a comprehensive Python-based system for macromolecular structure solution","volume":"66","author":"Adams","year":"2010","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"10.1016\/j.molcel.2023.10.038_bib67","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.molcel.2023.10.038_bib68","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1038\/s41467-022-28093-2","article-title":"The combined DNA and RNA synthetic capabilities of archaeal DNA primase facilitate primer hand-off to the replicative DNA polymerase","volume":"13","author":"Greci","year":"2022","journal-title":"Nat. Commun."}],"container-title":["Molecular Cell"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1097276523009097?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1097276523009097?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,22]],"date-time":"2025-10-22T00:55:01Z","timestamp":1761094501000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1097276523009097"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,12]]},"references-count":68,"journal-issue":{"issue":"23","published-print":{"date-parts":[[2023,12]]}},"alternative-id":["S1097276523009097"],"URL":"https:\/\/doi.org\/10.1016\/j.molcel.2023.10.038","relation":{},"ISSN":["1097-2765"],"issn-type":[{"value":"1097-2765","type":"print"}],"subject":[],"published":{"date-parts":[[2023,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Structural insights into the assembly and mechanism of mpox virus DNA polymerase complex F8-A22-E4-H5","name":"articletitle","label":"Article Title"},{"value":"Molecular Cell","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.molcel.2023.10.038","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"https:\/\/doi.org\/10.1016\/S0014-5793(01)03144-1","name":"associatedlink","label":"CrossRef DOI link to the associated document"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2023 Elsevier Inc.","name":"copyright","label":"Copyright"}]}}