{"code":"SASDEQ4","status":"Published","type_of_curve":"Single concentration","angular_unit":"1/A","project":{"title":"Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis.","publication":{"title":"Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis.","author_list":"Furlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL","journal":"Acta Crystallogr D Struct Biol","doi":"10.1107/S2059798319000081","pmid":"30950400","published_date":"2019 Mar 1"},"status":"released","submitted_date":"2018-09-18","released_date":"2019-03-29"},"pddf_data":"https://www.sasbdb.org/media/p_of_R_files/SASDEQ4.out","intensities_data":"https://www.sasbdb.org/media/intensities_files/SASDEQ4.dat","intensities_log_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDEQ4_dat_img.png","intensities_kratky_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDEQ4_kratky_img.png","pddf_plot":"https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDEQ4_pofr_img.png","intensities_guinier_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDEQ4_guinier_img.png","sascif_data":"https://www.sasbdb.org/media/sascif/sascif_files/SASDEQ4.sascif","experiment":{"instrument":{"detector":{"type":"Dectris","name":"Pilatus 1M","resolution":172.0},"name":"Australian  Synchrotron","city":"Melbourne","country":"Australia","beamline_name":"SAXS/WAXS","beam_geometry":"Point","type_of_source":"X-ray synchrotron","point_source":true,"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":"Deletion mutant of PmScsC","short_name":"PmScsC&Delta;L","sequence":"SNAALNAAQEKEVRALVRDTLVSNPEILEEAIMALQTKALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQYPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKSTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAKVKK","organism":"Proteus mirabilis","uniprot_code":"A0A1Z1SYD5","uniprot_range_first":22,"uniprot_range_last":243,"oligomerization":"unknown","molecular_type":"protein","uniprot_sequence":"MKKTLSVLVISSLLFGANVQAAALNAAQEKEVRALVRDTLVSNPEILEEAIMALQTKKAD\nEQQAQFRQALASEHDALYNDAASPRIGAKDAKLVLVSFTDYNCPYCKRFDPLLEKITEQY\nPDVAVIIKPLPFKGESSAKASQAVLSVWKEDPKAFLALHQRLMQKKTMLDNASIEDAMKS\nTNTSKIKLTDDSLKTLQNNLELSRKLGIQGTPATVIGDTILPGAVDYDQLEIIVKEQLAK\nVKK","mw":23.438,"total_mw":23.438,"number_molecules":0,"complex_state":false,"deuteration":null,"molecule_source":"biological","molecule_description":null}],"buffer":{"name":"10mM HEPES, 150mM NaCl","concentration_unit":null,"comment":null,"additive":null,"concentration":null,"pka":null,"ph":7.4,"deuteration":null},"purity_method":null,"name":"Deletion mutant of the suppressor of copper sensitivity C protein, PmScsC, with concentration series data","ext_coefficient":null,"contrast":null,"specific_vol":null,"dry_vol":null,"absorbption":null,"deuteration":null,"mixture":null},"contributor":[{"affiliation":[{"short_name":"ANSTO","address":"Kirrawee DC, NSW 2232, Australia","full_name":"Australian Nuclear Science and Technology Organisation","webpage":""}],"contributor_name":"Andrew","contributor_surname":"Whitten","orcid":null}],"concentration_method":null,"concentration_unit":null,"date":"2018-04-05","storage_temperature":4.0,"cell_temperature":10.0,"exposure_time":1.0,"number_of_frames":38,"wavelength":0.1033,"sample_detector_distance":3.33,"concentration_min":null,"concentration_max":10.0,"sample_volume":null,"flow_rate":null,"s_min":0.16,"s_max":3.634,"total_exposure_time":null,"seccolumn":null},"fits":[{"models":[{"model_plot":"https://www.sasbdb.org/media/pdb_file/images/SASDEQ4_fit1_model1_img.png","software":"PDB (Protein Data Bank)","pdb_link":[{"pdb_code":"4xvw","ext_code":"4XVW","ext_type":"pdb","difference_with_model":"identical"},{"pdb_code":"6mhh","ext_code":"6MHH","ext_type":"pdb","difference_with_model":"identical"}],"model_title":null,"type_of_model":"mix","software_version":null,"model_data":"https://www.sasbdb.org/media/pdb_file/SASDEQ4_fit1_model1.pdb","model_mw":69.23,"bead_radius":null,"log":null,"symmetry":"P3","comment":"Monomer, dimer and trimer structures are all derived from this PDB (yet to be deposited)","user":111}],"fit_unit":"1/A","fit_plot":"https://www.sasbdb.org/media/fitting_files/scattering_plots/PmScsCDL_10p0_nZbPwQE_fit_img.png","software":"Other","chi_square_value":177.8886,"p_value":0.0,"fit_residual_plot":"PmScsCDL_10p0_nZbPwQE_fitresiduals_img.png","fit_data":"https://www.sasbdb.org/media/fitting_files/SASDEQ4_fit1.fit","fit_log":null,"software_version":"1","description":"Fit from a linear combination of scattering profiles from monomeric, dimeric and trimeric PmScsC&Delta;L"}],"estimated_volume_method":null,"pddf_software":"ATSAS GNOM","pddf_software_version":"4.6","i0_calibration_standard":null,"description":null,"experiment_description":"X-ray synchrotron radiation scattering data from solutions of a deletion mutant of Suppressor of Copper Sensitivity C protein (ScsC) protein from Proteus mirabilis in 10 mM HEPES 150mM NaCl, pH 7.4 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Thirty eight successive 1 second frames were collected across solute concentrations of 0.1-10.0 mg/ml at a sample temperature of 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The SAXS data displayed this entry was derived from a 10.0 mg/ml sample and show that a mixture of monomer, dimer and trimer is present in solution. A linear combination of monomer, dimer and trimer are fit to the scattering curve, and the final concentration of each species in solution was determined to be: 122.70 µM (monomer); 73.15 µM (dimer); 12.29 µM (trimer). Together, with data collected at other concentration (available to download as a zip archive), it was estimated that K1 (monomer <-> dimer) was 205.81 µM, and K2 (monomer + dimer <-> trimer) 729.98 µM.","tags":[],"intensity_unit":"1/cm","experimental_mw":44.3,"experimental_mw_error":null,"guinier_i0_mw":null,"guinier_i0_mw_error":null,"porod_mw":null,"porod_mw_error":null,"pddf_i0":0.2413,"pddf_i0_error":0.0001,"guinier_i0":0.2423,"guinier_i0_error":0.0001,"pddf_rg":2.6,"pddf_rg_error":0.01,"guinier_rg":2.62,"guinier_rg_error":0.01,"pddf_dmax":9.0,"pddf_dmax_error":5.0,"porod_volume":54.0,"porod_volume_error":null,"estimated_volume":null,"estimated_volume_error":null,"guinier_point_first":1,"guinier_point_last":19,"pddf_point_first":null,"pddf_point_last":null,"i0_calibration_standard_data":null,"intensities_log_log_plot":"SASDEQ4_datloglog_img.png","symmetry":null,"last_modified":"2020-11-27T11:55:50.587847+01:00","bragg_peak":[]}