查看完整 summary.json 原文
{
"code": "SASDDC6",
"status": "Published",
"type_of_curve": "Merged",
"angular_unit": "1/nm",
"project": {
"title": "Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.",
"publication": {
"title": "Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control.",
"author_list": "Martínez-Lumbreras S, Krysztofinska EM, Thapaliya A, Spilotros A, Matak-Vinkovic D, Salvadori E, Roboti P, Nyathi Y, Muench JH, Roessler MM, Svergun DI, High S, Isaacson RL",
"journal": "BMC Biol",
"doi": "10.1186/s12915-018-0542-3",
"pmid": "29996828",
"published_date": "2018 Jul 11"
},
"status": "released",
"submitted_date": "2018-05-02",
"released_date": "2018-06-11"
},
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"sascif_data": "https://www.sasbdb.org/media/sascif/sascif_files/SASDDC6.sascif",
"experiment": {
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"name": "Pilatus 2M",
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},
"name": "PETRA III",
"city": "DESY; Hamburg",
"country": "Germany",
"beamline_name": "EMBL P12",
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"type_of_source": "X-ray synchrotron",
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"sample": {
"molecule": [
{
"long_name": "Small glutamine-rich tetratricopeptide repeat-containing protein alpha Nterminal-TPR domains",
"short_name": "SGTA_NT-TPR",
"sequence": "GSMDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPT",
"organism": "Homo sapiens",
"uniprot_code": "O43765",
"uniprot_range_first": 1,
"uniprot_range_last": 213,
"oligomerization": "dimer",
"molecular_type": "protein",
"uniprot_sequence": "MDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPE\nIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIEL\nNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVA\nYYKKALELDPDNETYKSNLKIAELKLREAPSPTGGVGSFDIAGLLNNPGFMSMASNLMNN\nPQIQQLMSGMISGGNNPLGTPGTSPSQNDLASLIQAGQQFAQQMQQQNPELIEQLRSQIR\nSRTPSASNDDQQE",
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"number_molecules": 2,
"complex_state": false,
"deuteration": null,
"molecule_source": "biological",
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}
],
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"concentration_unit": null,
"comment": null,
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"pka": null,
"ph": 6.0,
"deuteration": null
},
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"name": "Small glutamine-rich tetratricopeptide repeat-containing protein alpha (N-terminal-TPR domains; SGTA_NT)",
"ext_coefficient": null,
"contrast": null,
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"dry_vol": null,
"absorbption": null,
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"mixture": null
},
"contributor": [
{
"affiliation": [
{
"short_name": null,
"address": "London, UK",
"full_name": "King's College London",
"webpage": "https://www.kcl.ac.uk"
}
],
"contributor_name": "Rivka",
"contributor_surname": "Isaacson",
"orcid": null
}
],
"concentration_method": null,
"concentration_unit": null,
"date": "2015-06-05",
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"cell_temperature": 25.0,
"exposure_time": 0.045,
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"wavelength": 0.124,
"sample_detector_distance": 3.0,
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"description": null,
"experiment_description": "Synchrotron SAXS data from solutions of the small glutamine-rich tetratricopeptide repeat-containing protein alpha (N-terminal-TPR domains; SGTA_NT) in 10 mM potassium phosphate, 100 mM NaCl, pH 6, were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY, Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.6 and 4.5 mg/ml were measured at 25°C. 20 successive 0.045 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.",
"tags": [],
"intensity_unit": null,
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"intensities_log_log_plot": "SASDDC6_datloglog_img.png",
"symmetry": null,
"last_modified": "2023-06-21T07:56:39.492710+02:00",
"bragg_peak": []
}
查看完整 manifest.json 原文
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