Complex with 1H histone acetyltransferase Rtt109 and histones H3 and H4, 2H histone chaperones Asf1 and Vps75 (1H Rtt109-H3:H4, 2H Asf1-Vps75) acquired in 42% v/v D2O

{
  "code": "SASDFQ3",
  "status": "Published",
  "type_of_curve": "Single concentration",
  "angular_unit": "1/A",
  "project": {
    "title": "Histone chaperone exploits intrinsic disorder to switch acetylation specificity.",
    "publication": {
      "title": "Histone chaperone exploits intrinsic disorder to switch acetylation specificity.",
      "author_list": "Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T",
      "journal": "Nat Commun",
      "doi": "10.1038/s41467-019-11410-7",
      "pmid": "31387991",
      "published_date": "2019 Aug 6"
    },
    "status": "released",
    "submitted_date": "2019-02-27",
    "released_date": "2019-07-10"
  },
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  "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDFQ3.sascif",
  "experiment": {
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        "name": "6Li-Scintillator 1 mm thickness + photomultiplier",
        "resolution": 5.3
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      "name": "FRM2",
      "city": "Munich",
      "country": "Germany",
      "beamline_name": "KWS1",
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      "type_of_source": "neutron source",
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      "line_collimation_integrationwidth": null,
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          "long_name": "Vacuolar protein sorting-associated protein 75 (1-225 aa)",
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          "short_name": "H3 (35-135)",
          "sequence": "VKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAY \r\nLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA",
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          "uniprot_code": "P84233",
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    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": "Germany",
            "full_name": "Leibniz University of Hannover",
            "webpage": "https://www.uni-hannover.de"
          }
        ],
        "contributor_name": "Nataliya",
        "contributor_surname": "Danilenko",
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    "date": "2017-03-05",
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