{"code":"SASDVZ5","status":"Published","type_of_curve":"Single concentration","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 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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,"sample_volume":null,"flow_rate":null,"s_min":0.066,"s_max":6.854,"total_exposure_time":null,"seccolumn":null},"fits":[{"models":[{"model_plot":"https://www.sasbdb.org/media/pdb_file/images/SASDVZ5_fit1_model1_img.png","software":"DAMMIF","pdb_link":[],"model_title":null,"type_of_model":"dummy","software_version":"dammif (r3203)","model_data":"https://www.sasbdb.org/media/pdb_file/SASDVZ5_fit1_model1.pdb","model_mw":227.5,"bead_radius":2.5,"log":"https://www.sasbdb.org/media/log_files/1_7.48mg_1-7_uYHNtVa.log","symmetry":null,"comment":null,"user":1034}],"fit_unit":"1/A","fit_plot":"https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDVZ5_fit1_fixed_fit_img.png","software":"DAMMIF","chi_square_value":2.157961,"p_value":0.0,"fit_residual_plot":"SASDVZ5_fit1_fitresiduals_img.png","fit_data":"https://www.sasbdb.org/media/fitting_files/SASDVZ5_fit1.fir","fit_log":"https://www.sasbdb.org/media/fitting_files/log_files/1_7.48mg_1-7_9uFrvmW.log","software_version":"dammif (r3203)","description":""}],"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":[],"intensity_unit":"arbitrary","experimental_mw":229.0,"experimental_mw_error":null,"guinier_i0_mw":null,"guinier_i0_mw_error":null,"porod_mw":227.1,"porod_mw_error":null,"pddf_i0":1.064,"pddf_i0_error":null,"guinier_i0":8.03743,"guinier_i0_error":null,"pddf_rg":3.96,"pddf_rg_error":null,"guinier_rg":4.058,"guinier_rg_error":0.161,"pddf_dmax":11.77,"pddf_dmax_error":null,"porod_volume":375.0,"porod_volume_error":null,"estimated_volume":null,"estimated_volume_error":null,"guinier_point_first":4,"guinier_point_last":18,"pddf_point_first":null,"pddf_point_last":null,"i0_calibration_standard_data":null,"intensities_log_log_plot":"SASDVZ5_datloglog_img.png","symmetry":null,"last_modified":"2024-09-11T17:07:38.499123+02:00","bragg_peak":[]}