Human DNA repair protein RAD52 homolog (amino acids 1-212)

{
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  "angular_unit": "1/A",
  "project": {
    "title": "A glimpse into the hidden world of the flexible C-terminal protein binding domains of human RAD52",
    "publication": {
      "title": "A glimpse into the hidden world of the flexible C-terminal protein binding domains of human RAD52",
      "author_list": "Struble L, Lovelace J, Borgstahl G",
      "journal": "Journal of Structural Biology",
      "doi": "10.1016/j.jsb.2024.108115",
      "pmid": null,
      "published_date": "2024 Sep"
    },
    "status": "released",
    "submitted_date": "2024-08-07",
    "released_date": "2024-08-08"
  },
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      "detector": {
        "type": "Photon Counter",
        "name": "Pilatus 100K-S",
        "resolution": 172.0
      },
      "name": "Eppley Structural Biology Facility, University of Nebraska Medical Center",
      "city": "Omaha, NE",
      "country": "United States of America",
      "beamline_name": "Rigaku BioSAXS 1000",
      "beam_geometry": null,
      "type_of_source": "X-ray in house",
      "point_source": null,
      "line_collimation": null,
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    },
    "sample": {
      "molecule": [
        {
          "long_name": "DNA repair protein RAD52 homolog",
          "short_name": "RAD52",
          "sequence": "MSGTEEAILGGRDSHPAAGGGSVLCFGQCQYTAEEYQAIQKALRQRLGPEYISSRMAGGGQKVCYIEGHRVINLANEMFGYNGWAHSITQQNVDFVDLNNGKFYVGVCAFVRVQLKDGSYHEDVGYGVSEGLKSKALSLEKARKEAVTDGLKRALRSFGNALGNCILDKDYLRSLNKLPRQLPLEVDLTKAKRQDLEPSVEEARYNSCRPNM",
          "organism": "Homo sapiens",
          "uniprot_code": "P43351",
          "uniprot_range_first": 1,
          "uniprot_range_last": 212,
          "oligomerization": "decamer",
          "molecular_type": "protein",
          "uniprot_sequence": "MSGTEEAILGGRDSHPAAGGGSVLCFGQCQYTAEEYQAIQKALRQRLGPEYISSRMAGGG\nQKVCYIEGHRVINLANEMFGYNGWAHSITQQNVDFVDLNNGKFYVGVCAFVRVQLKDGSY\nHEDVGYGVSEGLKSKALSLEKARKEAVTDGLKRALRSFGNALGNCILDKDYLRSLNKLPR\nQLPLEVDLTKAKRQDLEPSVEEARYNSCRPNMALGHPQLQQVTSPSRPSHAVIPADQDCS\nSRSLSSSAVESEATHQRKLRQKQLQQQFRERMEKQQVRVSTPSAEKSEAAPPAPPVTHST\nPVTVSEPLLEKDFLAGVTQELIKTLEDNSEKWAVTPDAGDGVVKPSSRADPAQTSDTLAL\nNNQMVTQNRTPHSVCHQKPQAKSGSWDLQTYSADQRTTGNWESHRKSQDMKKRKYDPS",
          "mw": 23.4,
          "total_mw": 234.0,
          "number_molecules": 10,
          "complex_state": false,
          "deuteration": null,
          "molecule_source": "biological",
          "molecule_description": "The crystallisable N-terminal half of the hRAD52 protein."
        }
      ],
      "buffer": {
        "name": "20 mM Bis-Tris, 10% glycerol, 400 mM NaCl, 100 mM KCl, 1 mM EDTA",
        "concentration_unit": null,
        "comment": null,
        "additive": null,
        "concentration": null,
        "pka": null,
        "ph": 6.0,
        "deuteration": null
      },
      "purity_method": null,
      "name": "Human DNA repair protein RAD52 homolog (amino acids 1-212)",
      "ext_coefficient": null,
      "contrast": null,
      "specific_vol": null,
      "dry_vol": null,
      "absorbption": null,
      "deuteration": null,
      "mixture": null
    },
    "contributor": [
      {
        "affiliation": [
          {
            "short_name": null,
            "address": null,
            "full_name": "University of Nebraska Medical Center",
            "webpage": null
          }
        ],
        "contributor_name": "Lucas",
        "contributor_surname": "Struble",
        "orcid": "https://orcid.org/0000-0002-0671-259X"
      }
    ],
    "concentration_method": null,
    "concentration_unit": null,
    "date": "2014-07-25",
    "storage_temperature": 15.0,
    "cell_temperature": 15.0,
    "exposure_time": 9000.0,
    "number_of_frames": 1,
    "wavelength": 0.154,
    "sample_detector_distance": 0.48,
    "concentration_min": null,
    "concentration_max": 7.48,
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    "flow_rate": null,
    "s_min": 0.066,
    "s_max": 6.854,
    "total_exposure_time": null,
    "seccolumn": null
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      "chi_square_value": 2.157961,
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  "estimated_volume_method": null,
  "pddf_software": "ATSAS GNOM",
  "pddf_software_version": "4.5a",
  "i0_calibration_standard": null,
  "description": "Using SEC-MALS the molecular weight is closest to that expected for a 10-mer. The data used to calculate the P(r) profile, and subsequent DAM modelling has been normalized to protein concentration in mg/mL.",
  "experiment_description": "SAXS data from solutions of the human DNA repair protein RAD52 homolog (amino acids 1-212) in 20 mM Bis-Tris, 10% glycerol, 400 mM NaCl, 100 mM KCl, 1 mM EDTA, pH 6 were collected using a Rigaku/ BioSAXS1000 instrument at the Eppley Structural Biology Facility (University of Nebraska Medical Center, Omaha, NE, USA) equipped with a Dectris/Pilatus 100K-S detector at a sample-detector distance of 0.5 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 7.48 mg/ml was measured at 15°C. One 9000 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.",
  "tags": [],
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  "experimental_mw_error": null,
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  "guinier_i0_mw_error": null,
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  "pddf_rg_error": null,
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  "guinier_rg_error": 0.161,
  "pddf_dmax": 11.77,
  "pddf_dmax_error": null,
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  "porod_volume_error": null,
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  "guinier_point_first": 4,
  "guinier_point_last": 18,
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  "symmetry": null,
  "last_modified": "2024-09-11T17:07:38.499123+02:00",
  "bragg_peak": []
}

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