{"code":"SASDCM7","status":"Published","type_of_curve":"Other","angular_unit":"1/A","project":{"title":"Structural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors.","publication":{"title":"Structural Dynamics Control Allosteric Activation of Cytohesin Family Arf GTPase Exchange Factors.","author_list":"Malaby AW, Das S, Chakravarthy S, Irving TC, Bilsel O, Lambright DG","journal":"Structure","doi":"10.1016/j.str.2017.11.019","pmid":"29276036","published_date":"2018 Jan 2"},"status":"released","submitted_date":"2017-09-22","released_date":"2018-01-02"},"pddf_data":"https://www.sasbdb.org/media/p_of_R_files/SASDCM7.out","intensities_data":"https://www.sasbdb.org/media/intensities_files/SASDCM7.dat","intensities_log_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDCM7_dat_img.png","intensities_kratky_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDCM7_kratky_img.png","pddf_plot":"https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDCM7_pofr_img.png","intensities_guinier_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDCM7_guinier_img.png","sascif_data":"https://www.sasbdb.org/media/sascif/sascif_files/SASDCM7.sascif","experiment":{"instrument":{"detector":{"type":null,"name":"MAR 165 CCD","resolution":null},"name":"Advanced Photon Source (APS), Argonne National Laboratory","city":"Lemont, IL","country":"USA","beamline_name":"BioCAT 18ID","beam_geometry":null,"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":"Grp1 63-399 E161A 6GS Arf6 Q67L fusion protein","short_name":null,"sequence":"MGHHHHHHGSTTQRNAQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLNKTVIGDYLGER\r\nDDFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAFASRYCLCNPGVFQSTDTCYVL\r\nSFAIIMLNTSLHNHNVRDKPTAERFITMNRGINEGGDLPEELLRNLYESIKNEPFKIPEDDGNDLTHTFFNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSH\r\nKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKKGSGSGSGSGSGSGKVLSKIFGNKEMRILM\r\nLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNVWDVGGLDKIRPLWRHYYTGTQGLIFVV\r\nDCADRDRIDEARQELHRIINDREMRDAIILIFANKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATS\r\nGDGLYEGLTWLTSNYN","organism":"Mus musculus","uniprot_code":null,"uniprot_range_first":null,"uniprot_range_last":null,"oligomerization":"monomer","molecular_type":"protein","uniprot_sequence":null,"mw":61.011,"total_mw":61.011,"number_molecules":1,"complex_state":false,"deuteration":null,"molecule_source":"biological","molecule_description":null}],"buffer":{"name":"20 mM Tris, 150 mM NaCl, 2 mM MgCl2, 0.1% 2-mercaptoethanol, 5% glycerol, 0.001 mM insitol 1,3,4,5-tetrakis phosphate","concentration_unit":null,"comment":null,"additive":null,"concentration":null,"pka":null,"ph":8.0,"deuteration":null},"purity_method":null,"name":"Truncated monomeric Cytohesin-3 (Grp1; amino acids 63-399) E161A 6GS Arf6 Q67L fusion protein","ext_coefficient":null,"contrast":null,"specific_vol":null,"dry_vol":null,"absorbption":null,"deuteration":null,"mixture":null},"contributor":[{"affiliation":[{"short_name":"UMASS","address":"Worcester, MA, USA","full_name":"UMASS Medical School","webpage":"https://www.umassmed.edu/"}],"contributor_name":"David","contributor_surname":"Lambright","orcid":null}],"concentration_method":null,"concentration_unit":null,"date":"2013-11-15","storage_temperature":null,"cell_temperature":20.0,"exposure_time":1.0,"number_of_frames":1,"wavelength":0.10332,"sample_detector_distance":2.5,"concentration_min":0.0,"concentration_max":2.4,"sample_volume":null,"flow_rate":null,"s_min":0.069,"s_max":3.327,"total_exposure_time":null,"seccolumn":null},"fits":[{"models":[{"model_plot":"https://www.sasbdb.org/media/pdb_file/images/SASDCM7_fit1_model1_img.png","software":"DAMMIF","pdb_link":[],"model_title":null,"type_of_model":"dummy","software_version":"r2835","model_data":"https://www.sasbdb.org/media/pdb_file/SASDCM7_fit1_model1.pdb","model_mw":53.0,"bead_radius":3.0,"log":"https://www.sasbdb.org/media/log_files/dammif-60.log","symmetry":"P1","comment":"Most representative of 100 dammif models","user":241},{"model_plot":"https://www.sasbdb.org/media/pdb_file/images/SASDCM7_fit1_model2_img.png","software":"DAMFILT","pdb_link":[],"model_title":null,"type_of_model":"dummy","software_version":"","model_data":"https://www.sasbdb.org/media/pdb_file/SASDCM7_fit1_model2.pdb","model_mw":54.387,"bead_radius":2.75,"log":null,"symmetry":"P1","comment":"Filtered average of 10 filtered averages of 10 dammif models","user":241}],"fit_unit":"1/A","fit_plot":"https://www.sasbdb.org/media/fitting_files/scattering_plots/SASDCM7_fit1_fit_img.png","software":"DAMMIF","chi_square_value":1.05,"p_value":0.1297,"fit_residual_plot":"SASDCM7_fit1_fitresiduals_img.png","fit_data":"https://www.sasbdb.org/media/fitting_files/SASDCM7_fit1.fir","fit_log":"https://www.sasbdb.org/media/fitting_files/log_files/dammif-60.log","software_version":"r2835","description":null}],"estimated_volume_method":null,"pddf_software":"ATSAS GNOM","pddf_software_version":"5.0","i0_calibration_standard":null,"description":null,"experiment_description":"This experimental profile was derived from SEC-SAXS data collected at the BioCAT Sector 18-ID beamline at the Argonne National Laboratory Advanced Photon Source using a MAR 165 CCD detector.  The protein was equilibrated with a 1.2 molar excess of inositol 1,3,4,5-tetrakis phosphate (IP4), concentrated to 10 mg/ml, and injected in 0.1 ml onto a 3 ml Superdex-200 Increase column equilibrated with 20 mM Tris, pH 8.0, 150 mM NaCl, 2 mM MgCl2, 0.1% 2-mercaptoethanol, 5% glycerol, and 0.001 ml IP4.  SAXS data sets were acquired with 1 s exposures at 5 s intervals during elution at a flow rate of 0.25 ml/min.  Raw SAXS images were radially averaged on a log scale over the q range 0.00621-0.333 Å-1 and normalized by the incident beam intensity.  The protein scattering profile was reconstructed by singular value decomposition and linear combination (SVD-LC) as described in Malaby et al. (2015) Methods for analysis of size-exclusion chromatography-small angle X-ray scattering and reconstruction of protein scattering. J Appl Crystallogr 48: 1102-1113.","tags":[],"intensity_unit":"arbitrary","experimental_mw":61.9,"experimental_mw_error":null,"guinier_i0_mw":null,"guinier_i0_mw_error":null,"porod_mw":61.9,"porod_mw_error":null,"pddf_i0":1.02,"pddf_i0_error":0.001,"guinier_i0":1.02,"guinier_i0_error":0.001,"pddf_rg":3.29,"pddf_rg_error":0.008,"guinier_rg":3.27,"guinier_rg_error":0.01,"pddf_dmax":11.9,"pddf_dmax_error":0.1,"porod_volume":92.8,"porod_volume_error":null,"estimated_volume":null,"estimated_volume_error":null,"guinier_point_first":1,"guinier_point_last":30,"pddf_point_first":null,"pddf_point_last":null,"i0_calibration_standard_data":null,"intensities_log_log_plot":"SASDCM7_datloglog_img.png","symmetry":null,"last_modified":"2019-12-06T13:07:15.624532+01:00","bragg_peak":[]}