{"code":"SASDFX4","status":"Published","type_of_curve":"SEC-SAS","angular_unit":"1/A","project":{"title":"How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids.","publication":{"title":"How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids.","author_list":"Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O","journal":"J Struct Biol","doi":"10.1016/j.jsb.2019.107411","pmid":"31689503","published_date":"2019 Nov 2"},"status":"released","submitted_date":"2019-03-30","released_date":"2019-11-14"},"pddf_data":"https://www.sasbdb.org/media/p_of_R_files/SASDFX4.out","intensities_data":"https://www.sasbdb.org/media/intensities_files/SASDFX4.dat","intensities_log_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFX4_dat_img.png","intensities_kratky_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFX4_kratky_img.png","pddf_plot":"https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDFX4_pofr_img.png","intensities_guinier_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDFX4_guinier_img.png","sascif_data":"https://www.sasbdb.org/media/sascif/sascif_files/SASDFX4.sascif","experiment":{"instrument":{"detector":{"type":"CCD","name":"AVIEX PCCD170170","resolution":null},"name":"SOLEIL","city":"Saint-Aubin","country":"France","beamline_name":"SWING","beam_geometry":"","type_of_source":"X-ray synchrotron","point_source":null,"line_collimation":null,"sample_path_length":null,"line_collimation_slitlength":null,"line_collimation_integrationwidth":null,"xray_energy":null,"beam_profile_ah":null,"beam_profile_al":null},"sample":{"molecule":[{"long_name":"Human dystrophin central domain R11-19 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GRNTPGKPMREDTM","mw":116.685,"total_mw":116.685,"number_molecules":1,"complex_state":false,"deuteration":null,"molecule_source":"biological","molecule_description":null}],"buffer":{"name":"NaP 20 mM, NaCl 300 mM, EDTA 1 mM, Glycerol 2%","concentration_unit":null,"comment":null,"additive":null,"concentration":null,"pka":null,"ph":7.5,"deuteration":null},"purity_method":null,"name":"Conformation of R11-19 human dystrophin fragment","ext_coefficient":null,"contrast":null,"specific_vol":null,"dry_vol":null,"absorbption":null,"deuteration":null,"mixture":null},"contributor":[{"affiliation":[{"short_name":null,"address":"France","full_name":"University of Lorraine","webpage":"http://welcome.univ-lorraine.fr/"}],"contributor_name":"Raphael","contributor_surname":"Dos Santos Morais","orcid":""}],"concentration_method":null,"concentration_unit":null,"date":"2017-05-11","storage_temperature":null,"cell_temperature":15.0,"exposure_time":0.75,"number_of_frames":21,"wavelength":0.1033,"sample_detector_distance":1.8,"concentration_min":null,"concentration_max":null,"sample_volume":null,"flow_rate":null,"s_min":0.062,"s_max":6.143,"total_exposure_time":null,"seccolumn":null},"fits":[{"models":[{"model_plot":"https://www.sasbdb.org/media/pdb_file/images/SASDFX4_fit1_model1_img.png","software":"Custom in-house","pdb_link":[],"model_title":null,"type_of_model":"atomic","software_version":null,"model_data":"https://www.sasbdb.org/media/pdb_file/SASDFX4_fit1_model1.pdb","model_mw":112.7,"bead_radius":null,"log":null,"symmetry":null,"comment":null,"user":427}],"fit_unit":"1/A","fit_plot":"https://www.sasbdb.org/media/fitting_files/scattering_plots/model1R11-R19_fixed_fit_img.png","software":"CRYSOL","chi_square_value":12.122,"p_value":0.0,"fit_residual_plot":null,"fit_data":"https://www.sasbdb.org/media/fitting_files/SASDFX4_fit1.fit","fit_log":null,"software_version":null,"description":""}],"estimated_volume_method":null,"pddf_software":"ATSAS GNOM","pddf_software_version":"4.6","i0_calibration_standard":null,"description":"SEC-SAXS was performed at 15°C using the following parameters: Column: BioSEC5-500A (4.6 mm id * 300 mm); Flow rate: 0.3 mL/min; Sample injection concentration: 4.5 mg/mL; Injection volume: 70 μL. The data were collected through the SEC peak of the protein as a series of 21 x 1.5 second exposures.\r\nThe experimental molecular weight was determined from the volume of correlation, Vc.","experiment_description":"Synchrotron SAXS data from solutions of the R11-19 human dystrophin fragment in NaP 20 mM, NaCl 300 mM, EDTA 1 mM, glycerol 2%, pH 7.5 were collected using size-exclusion chromatography SAXS (SEC-SAXS) on the SWING beam line at SOLEIL (Saint-Aubin, France) using a CCD AVIEX PCCD170170 detector at a sample-detector distance of 1.8 m and at a wavelength of λ = 0.1033 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). 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":120.0,"experimental_mw_error":null,"guinier_i0_mw":null,"guinier_i0_mw_error":null,"porod_mw":null,"porod_mw_error":null,"pddf_i0":1.08,"pddf_i0_error":null,"guinier_i0":1.08,"guinier_i0_error":0.01,"pddf_rg":9.14,"pddf_rg_error":null,"guinier_rg":8.83,"guinier_rg_error":0.13,"pddf_dmax":37.5,"pddf_dmax_error":null,"porod_volume":513.0,"porod_volume_error":null,"estimated_volume":null,"estimated_volume_error":null,"guinier_point_first":1,"guinier_point_last":11,"pddf_point_first":null,"pddf_point_last":null,"i0_calibration_standard_data":null,"intensities_log_log_plot":"SASDFX4_datloglog_img.png","symmetry":null,"last_modified":"2019-12-06T13:07:15.624532+01:00","bragg_peak":[]}