{"code":"SASDD37","status":"Published","type_of_curve":"Single concentration","angular_unit":"1/A","project":{"title":"FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants.","publication":{"title":"FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants.","author_list":"Grinter R, Hay ID, Song J, Wang J, Teng D, Dhanesakaran V, Wilksch JJ, Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T","journal":"PLoS Biol","doi":"10.1371/journal.pbio.2006026","pmid":"30071011","published_date":"2018 Aug"},"status":"released","submitted_date":"2018-05-19","released_date":"2018-06-13"},"pddf_data":"https://www.sasbdb.org/media/p_of_R_files/SASDD37.out","intensities_data":"https://www.sasbdb.org/media/intensities_files/SASDD37.dat","intensities_log_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDD37_dat_img.png","intensities_kratky_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDD37_kratky_img.png","pddf_plot":"https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDD37_pofr_img.png","intensities_guinier_plot":"https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDD37_guinier_img.png","sascif_data":"https://www.sasbdb.org/media/sascif/sascif_files/SASDD37.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":"Ferredoxin protease E83A mutant","short_name":"FusC E83A","sequence":"EEIKSPLPVFKEGTLANGFRYTLVQLEGPKTRVDIRLIVDVGSIDEKDNESGVAH\r\nMVAHMVFRASDAFPQGVSTELHKQGWGRGQSYNAVTNYERTMYMMSPPKGNLDLGATLQALSQMTGHAKLLQSDLDDERK\r\nIILEEWRGKLGVAERMNQQRVQAIRHDSRYPSRPVIGTEESINDTPASVLQDFYQRWYHPSNMRLMIIGDITPADAEREI\r\nQRYFAALPNVAVPTRDYYEPLLKPQLKVARLQDSQSGSSQVSFVYRFNDKDAFGQSEYRHRLLTQITMSAVTRQVRRQKA\r\nELPQDASSLVVRKSDIGKTTAALGFFANVMPGGHDAAISAVLKEIERFKRYPLNEQDITEITSDIREVAQRMSVTPETRE\r\nFADWVQQLTIVWQQDRPYVGSQQRGKDALEALDTIKGEDVNRHWQRWLASPDTLAQFSVPGATPFTLPKPDAISKLQKQW\r\nALATLAPLRLEEKKIIPELPSVTQSGKRTAVKTFAAQKVEQWQLSNGDRVVWLRAPEAGKKVYLTATSQAGFMATAMNPW\r\nQAQLASQLVNQSGPATWSGESLSNWKKEKTLSLSIDQEADQLTLSGTAPTEQLASLFGLYRELNVAPGIDPDVMKESMMS\r\nLARQKANDDQSVGGKRASEMTKLRFGEPAWQQPEIAELKKISAPALLSQWHKAASAPVTYYLIADMPATQLLPQVERYLA\r\nTIPRQPASEVKQHLALSGKREATSAINVEPRADILTWSFTPHAWTPQAAVQVSIARNIASKYLKTSLRDDALGIYRMRVD\r\nSELEDKKQRIETEVSFTSAPERAQELWTLAEQAFSELPTKITQQDVDEQKAQFIRAEKGRQGDLTTIQRRLILSYRHYND\r\nPRYLSNASKLADSITLESVRAMSAKLYNPDNRVLYITLPQEVKE","organism":"Pectobacterium atrosepticum SCRI1043","uniprot_code":"Q6D8U3","uniprot_range_first":26,"uniprot_range_last":924,"oligomerization":"monomer","molecular_type":"protein","uniprot_sequence":"MNWKKCCWLSLTAVGLLAGSVVSQAEEIKSPLPVFKEGTLANGFRYTLVQLEGPKTRVDI\nRLIVDVGSIDEKDNESGVAHMVEHMVFRASDAFPQGVSTELHKQGWGRGQSYNAVTNYER\nTMYMMSPPKGNLDLGATLQALSQMTGHAKLLQSDLDDERKIILEEWRGKLGVAERMNQQR\nVQAIRHDSRYPSRPVIGTEESINDTPASVLQDFYQRWYHPSNMRLMIIGDITPADAEREI\nQRYFAALPNVAVPTRDYYEPLLKPQLKVARLQDSQSGSSQVSFVYRFNDKDAFGQSEYRH\nRLLTQITMSAVTRQVRRQKAELPQDASSLVVRKSDIGKTTAALGFFANVMPGGHDAAISA\nVLKEIERFKRYPLNEQDITEITSDIREVAQRMSVTPETREFADWVQQLTIVWQQDRPYVG\nSQQRGKDALEALDTIKGEDVNRHWQRWLASPDTLAQFSVPGATPFTLPKPDAISKLQKQW\nALATLAPLRLEEKKIIPELPSVTQSGKRTAVKTFAAQKVEQWQLSNGDRVVWLRAPEAGK\nKVYLTATSQAGFMATAMNPWQAQLASQLVNQSGPATWSGESLSNWKKEKTLSLSIDQEAD\nQLTLSGTAPTEQLASLFGLYRELNVAPGIDPDVMKESMMSLARQKANDDQSVGGKRASEM\nTKLRFGEPAWQQPEIAELKKISAPALLSQWHKAASAPVTYYLIADMPATQLLPQVERYLA\nTIPRQPASEVKQHLALSGKREATSAINVEPRADILTWSFTPHAWTPQAAVQVSIARNIAS\nKYLKTSLRDDALGIYRMRVDSELEDKKQRIETEVSFTSAPERAQELWTLAEQAFSELPTK\nITQQDVDEQKAQFIRAEKGRQGDLTTIQRRLILSYRHYNDPRYLSNASKLADSITLESVR\nAMSAKLYNPDNRVLYITLPQEVKE","mw":101.195,"total_mw":101.195,"number_molecules":1,"complex_state":false,"deuteration":null,"molecule_source":"biological","molecule_description":null},{"long_name":"Arabidopsis ferredoxin 2","short_name":"Ara_Fer2","sequence":"ATYKVKFITPEGELEVECDDDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSVDQSDQSFLDDEQIGEGFVLTCAAYPTSDVTIETHKEEAIMLEHHHHHH","organism":"Arabidopsis thaliana","uniprot_code":"P16972","uniprot_range_first":53,"uniprot_range_last":145,"oligomerization":"monomer","molecular_type":"protein","uniprot_sequence":"MASTALSSAIVGTSFIRRSPAPISLRSLPSANTQSLFGLKSGTARGGRVTAMATYKVKFI\nTPEGELEVECDDDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSVDQSDQSFLDDEQ\nIGEGFVLTCAAYPTSDVTIETHKEEDIV","mw":11.33,"total_mw":11.33,"number_molecules":1,"complex_state":false,"deuteration":null,"molecule_source":"biological","molecule_description":null}],"buffer":{"name":"20 mM Tris, 150 mM NaCl","concentration_unit":null,"comment":null,"additive":null,"concentration":null,"pka":null,"ph":7.8,"deuteration":null},"purity_method":null,"name":"The ferredoxin protease, FusC, E83A mutant + 70 µM Arabidopsis ferredoxin","ext_coefficient":null,"contrast":null,"specific_vol":null,"dry_vol":null,"absorbption":null,"deuteration":null,"mixture":null},"contributor":[{"affiliation":[{"short_name":null,"address":"Melbourne, Australia","full_name":"Monash University","webpage":"http://www.monash.edu/"}],"contributor_name":"Grinter","contributor_surname":"Grinter","orcid":"https://orcid.org/0000-0002-8195-5348"}],"concentration_method":null,"concentration_unit":null,"date":"2017-10-26","storage_temperature":20.0,"cell_temperature":20.0,"exposure_time":null,"number_of_frames":null,"wavelength":0.103,"sample_detector_distance":1.28,"concentration_min":null,"concentration_max":3.0,"sample_volume":null,"flow_rate":null,"s_min":0.114,"s_max":3.038,"total_exposure_time":null,"seccolumn":null},"fits":[],"estimated_volume_method":null,"pddf_software":"ATSAS GNOM","pddf_software_version":"5.0","i0_calibration_standard":null,"description":"The FusC E83A mutant (30 µM) in the presence of 70 µM Arabidopsis ferredoxin. The background subtraction included 70 µM Arabidopsis ferredoxin in buffer.","experiment_description":"Synchrotron SAXS data from solutions of ferredoxin protease, FusC, E83A mutant + 70 µM Arabidopsis ferredoxin in 20 mM Tris, 150 mM NaCl, pH 7.8 were collected on the SAXS/WAXS beam line at the Australian Synchrotron storage ring (Melbourne, Australia) using a Pilatus 1M detector at a sample-detector distance of 1.3 m and at a wavelength of λ = 0.103 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 20°C. 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":100.0,"experimental_mw_error":null,"guinier_i0_mw":null,"guinier_i0_mw_error":null,"porod_mw":96.9,"porod_mw_error":null,"pddf_i0":0.2707,"pddf_i0_error":null,"guinier_i0":0.28,"guinier_i0_error":0.00032,"pddf_rg":3.8,"pddf_rg_error":null,"guinier_rg":3.71,"guinier_rg_error":0.035,"pddf_dmax":13.95,"pddf_dmax_error":null,"porod_volume":164.8,"porod_volume_error":null,"estimated_volume":null,"estimated_volume_error":null,"guinier_point_first":12,"guinier_point_last":33,"pddf_point_first":null,"pddf_point_last":null,"i0_calibration_standard_data":null,"intensities_log_log_plot":"SASDD37_datloglog_img.png","symmetry":null,"last_modified":"2019-12-06T13:07:15.624532+01:00","bragg_peak":[]}