{"doi":"10.1017/s1431927600018328","title":"Atomic Force Microscopy (Afm) of Chromatin Fibers: What Can We Learn?","abstract":"<jats:title>Abstract</jats:title>\n               <jats:p>DNA in the eukaryotic nucleus is not naked. Instead, it is complexed at frequent intervals with an equal molecular mass of histones to form nucleosomes. In the nucleosome, ∼146 bp of DNA are wrapped around a core histone octamer composed of two copies each of histones H4, H3, H2B, and H2A. The family of linker histones (H1, H5 and H1°) bind to the DNA between successive nucleosomes and help maintain the three-dimensional arrangement of nucleosomes within the chromatin fiber. AFM studies of chromatin fibers with the histones either selectively trypsinized or selectively reconstituted demonstrate a specific role for the H3 N-termini in maintaining fiber structure, in conjunction with the 80 amino acid linker histone globular domain. These AFM results structurally agree with the location of the H3 N-termini in the histone octamer or the nucleosome core particle.</jats:p>","journal":"Microscopy and Microanalysis","year":1999,"id":13812,"datarank":0.0,"base_score":0.0,"endowment":0.0,"self_citation_contribution":0.0,"citation_network_contribution":0.0,"self_endowment_contribution":0.0,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":0,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":111755,"name":"R Bash","orcid":null,"position":1,"is_corresponding":false},{"id":111756,"name":"D Lohr","orcid":null,"position":2,"is_corresponding":false},{"id":111757,"name":"S M Lindsay","orcid":null,"position":3,"is_corresponding":false},{"id":111758,"name":"J Zlatanova","orcid":null,"position":4,"is_corresponding":false},{"id":111754,"name":"SH Leuba","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"18940862","pmcid":null,"openalex_id":"https://openalex.org/W3039495702","authors":[],"funders":[],"total_grants":0,"fwci":0.0,"citation_percentile":0.23259417,"influential_citations":0,"citation_trend":[],"oa_status":"closed","license":"https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model","oa_locations":[{"url":"https://academic.oup.com/mam/article-pdf/5/S2/1000/59059351/mam1000.pdf","host_type":"publisher"},{"url":"https://doi.org/10.1017/s1431927600018328","host_type":"journal"}],"fields_of_study":["Genomics and Chromatin Dynamics","RNA and protein synthesis mechanisms","RNA Research and Splicing","Materials Science","Biology","Physics"],"mesh_terms":[],"keywords":["Histone octamer","Nucleosome","Linker DNA","Chromatosome","Histone H1","Histone","Chromatin","Biophysics","Histone code","Histone H2A","Chemistry","DNA","Crystallography","Biology","Biochemistry"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-05-31T17:41:28.353260Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}