{ "code": "SASDV57", "status": "Published", "type_of_curve": "SEC-SAS", "angular_unit": "1/A", "project": { "title": "Structural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation", "publication": { "title": "Structural dynamics of IDR interactions in human SFPQ and implications for liquid–liquid phase separation", "author_list": "Koning H, Lai V, Sethi A, Chakraborty S, Ang C, Fox A, Duff A, Whitten A, Marshall A, Bond C", "journal": "Acta Crystallographica Section D Structural Biology", "doi": "10.1107/S2059798325005303", "pmid": null, "published_date": "2025 Jun 27" }, "status": "released", "submitted_date": "2024-09-18", "released_date": "2025-06-29" }, "pddf_data": "https://www.sasbdb.org/media/p_of_R_files/SASDV57.out", "intensities_data": "https://www.sasbdb.org/media/intensities_files/SASDV57.dat", "intensities_log_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDV57_dat_img.png", "intensities_kratky_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDV57_kratky_img.png", "pddf_plot": "https://www.sasbdb.org/media/p_of_R_files/pofr_images/SASDV57_pofr_img.png", "intensities_guinier_plot": "https://www.sasbdb.org/media/intensities_files/scattering_plots/SASDV57_guinier_img.png", "sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDV57.sascif", "experiment": { "instrument": { "detector": { "type": null, "name": "Pilatus3 S 2M", "resolution": 172.0 }, "name": "Australian Synchrotron", "city": "Melbourne", "country": "Australia", "beamline_name": "SAXS/WAXS", "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": "Splicing factor, proline- and glutamine-rich", "short_name": "SFPQ cysteine dimer", "sequence": "GAMSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPIPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPGVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGEPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLFVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGRQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFASKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRFAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLMRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRMGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGSDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF", "organism": "Homo sapiens", "uniprot_code": "P23246", "uniprot_range_first": 214, "uniprot_range_last": 707, "oligomerization": "dimer", "molecular_type": "protein", "uniprot_sequence": "MSRDRFRSRGGGGGGFHRRGGGGGRGGLHDFRSPPPGMGLNQNRGPMGPGPGQSGPKPPI\nPPPPPHQQQQQPPPQQPPPQQPPPHQPPPHPQPHQQQQPPPPPQDSSKPVVAQGPGPAPG\nVGSAPPASSSAPPATPPTSGAPPGSGPGPTPTPPPAVTSAPPGAPPPTPPSSGVPTTPPQ\nAGGPPPPPAAVPGPGPGPKQGPGPGGPKGGKMPGGPKPGGGPGLSTPGGHPKPPHRGGGE\nPRGGRQHHPPYHQQHHQGPPPGGPGGRSEEKISDSEGFKANLSLLRRPGEKTYTQRCRLF\nVGNLPADITEDEFKRLFAKYGEPGEVFINKGKGFGFIKLESRALAEIAKAELDDTPMRGR\nQLRVRFATHAAALSVRNLSPYVSNELLEEAFSQFGPIERAVVIVDDRGRSTGKGIVEFAS\nKPAARKAFERCSEGVFLLTTTPRPVIVEPLEQLDDEDGLPEKLAQKNPMYQKERETPPRF\nAQHGTFEYEYSQRWKSLDEMEKQQREQVEKNMKDAKDKLESEMEDAYHEHQANLLRQDLM\nRRQEELRRMEELHNQEMQKRKEMQLRQEEERRRREEEMMIRQREMEEQMRRQREESYSRM\nGYMDPRERDMRMGGGGAMNMGDPYGSGGQKFPPLGGGGGIGYEANPGVPPATMSGSMMGS\nDMRTERFGQGGAGPVGGQGPRGMGPGTPAGYGRGREEYEGPNKKPRF", "mw": 76.277, "total_mw": 152.554, "number_molecules": 2, "complex_state": false, "deuteration": null, "molecule_source": "biological", "molecule_description": "R542C mutation causes monomers of SFPQ to dimerise via the coiled-coil domain (Lee et al, 2015)" } ], "buffer": { "name": "500mM KNO3, 20mM HEPES, 5% glycerol, 1mM DTT", "concentration_unit": null, "comment": null, "additive": null, "concentration": null, "pka": null, "ph": 7.4, "deuteration": null }, "purity_method": null, "name": "Full-length SFPQ in high salt buffer", "ext_coefficient": null, "contrast": null, "specific_vol": null, "dry_vol": null, "absorbption": null, "deuteration": null, "mixture": null }, "contributor": [], "concentration_method": null, "concentration_unit": null, "date": "2022-10-22", "storage_temperature": 25.0, "cell_temperature": 25.0, "exposure_time": 1.0, "number_of_frames": 700, "wavelength": 0.10781, "sample_detector_distance": 2.79, "concentration_min": null, "concentration_max": 4.2, "sample_volume": 60.0, "flow_rate": 0.4, "s_min": 0.051, "s_max": 5.704, "total_exposure_time": null, "seccolumn": 2 }, "fits": [], "estimated_volume_method": null, "pddf_software": "ATSAS GNOM", "pddf_software_version": "5.0", "i0_calibration_standard": null, "description": "A dimer of full-length SFPQ at 4.2mg/ml in 500mM KNO3, 20mM HEPES (pH 7.4), 5% glycerol, 1mM DTT. \r\n\r\nMeasurement was taken at the Australian Synchrotron SAXS/WAXS beamline and is part of the manuscript ' Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation '.", "experiment_description": "Synchrotron SAXS data from solutions of Dimeric full-length human Splicing factor, proline- and glutamine-rich (SFPQ) in 500mM KNO3, 20mM HEPES, 5% glycerol, 1mM DTT, pH 7.4 were collected on the SAXS/WAXS beam line at the Australian Synchrotron storage ring (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.10781 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 60.00 μl sample at 4.2 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 25°C. 450 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. A dimer of full-length SFPQ at 4.2mg/ml in 500mM KNO3, 20mM HEPES (pH 7.4), 5% glycerol, 1mM DTT. Measurement was taken at the Australian Synchrotron SAXS/WAXS beamline and is part of the manuscript ' Structural dynamics of IDR interactions in human SFPQ and implications for liquid-liquid phase separation '.", "tags": [], "intensity_unit": "1/cm", "experimental_mw": 200.46, "experimental_mw_error": null, "guinier_i0_mw": null, "guinier_i0_mw_error": null, "porod_mw": 380.0, "porod_mw_error": null, "pddf_i0": 0.02728, "pddf_i0_error": null, "guinier_i0": 0.0259164, "guinier_i0_error": null, "pddf_rg": 9.5, "pddf_rg_error": null, "guinier_rg": 7.935, "guinier_rg_error": 1.807, "pddf_dmax": 42.5, "pddf_dmax_error": null, "porod_volume": 485.0, "porod_volume_error": null, "estimated_volume": null, "estimated_volume_error": null, "guinier_point_first": 3, "guinier_point_last": 31, "pddf_point_first": null, "pddf_point_last": null, "i0_calibration_standard_data": null, "intensities_log_log_plot": "SASDV57_datloglog_img.png", "symmetry": null, "last_modified": "2025-07-03T11:05:26.761664+02:00", "bragg_peak": [] }