查看完整 summary.json 原文
{
"code": "SASDBG3",
"status": "Published",
"type_of_curve": "Single concentration",
"angular_unit": "1/nm",
"project": {
"title": "Crystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding.",
"publication": {
"title": "Crystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding.",
"author_list": "Paatero A, Rosti K, Shkumatov AV, Sele C, Brunello C, Kysenius K, Singha P, Jokinen V, Huttunen H, Kajander T",
"journal": "Biochemistry",
"doi": "10.1021/acs.biochem.5b00971",
"pmid": "26785044",
"published_date": "2016 Feb 16"
},
"status": "released",
"submitted_date": "2016-01-25",
"released_date": "2016-01-26"
},
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"experiment": {
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"name": "Pilatus 1M",
"resolution": 172.0
},
"name": "ESRF",
"city": "Grenoble",
"country": "France",
"beamline_name": "ID14-3",
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{
"long_name": "Mouse Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)",
"short_name": "cLRRTM2 30-380",
"sequence": "GPMACPPKCRCEKLLFYCDSQGFHSVPNGLPSQLLGLSLRHNQLQSLPNGVFDKLTQLTWLHLDHNQLQSLPNGVFDKLTKLTELILSSNQLQSLPNGTFDKLTNLQNLDLSFNQLQSLPNGVFDKLTNLQTLHLRSNQLQSLPNGVFDKLTSLTFLDLSTNQLQSLPNGVFDKLTNLRELHLEHNQL QSLPNGVFDKLTSLTTLFLQWNQLQSLPNGVFDKLTNLEKLDLTGNQLQSLPNGVFDKLTNLKILLLDNNQLQSLPNGVFDKLKSLTTVGLSGNLWECSPRVCALASWLGSFQGRWEHSILCHSPDHTQGEDILDAVHGFQLCWNLSTTVTAMATTYRDPTTEKLVEKY\r\n",
"organism": "Mus musculus",
"uniprot_code": "Q8BGA3",
"uniprot_range_first": 30,
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"oligomerization": "monomer",
"molecular_type": "protein",
"uniprot_sequence": "MGLHFKWPLGAPMLAAIYAMSVVLKMLPALGMACPPKCRCEKLLFYCDSQGFHSVPNATD\nKGSLGLSLRHNHITALERDQFASFSQLTWLHLDHNQISTVKEDAFQGLYKLKELILSSNK\nIFYLPNTTFTQLINLQNLDLSFNQLSSLHPELFYGLRKLQTLHLRSNSLRTIPVRLFWDC\nRSLEFLDLSTNRLRSLARNGFAGLIKLRELHLEHNQLTKINFAHFLRLSSLHTLFLQWNK\nISNLTCGMDWTWSTLEKLDLTGNEIKAIDLTVFETMPNLKILLMDNNKLNSLDSKILNSL\nKSLTTVGLSGNLWECSPRVCALASWLGSFQGRWEHSILCHSPDHTQGEDILDAVHGFQLC\nWNLSTTVTAMATTYRDPTTEYTKISSSSYHVGDKEIPTTAGIAVTTEEHFPEPDNAIFTQ\nRVITGTMALLFSFFFIIFIVFISRKCCPPTLRRIRQCSMIQNHRQLRSQTRLHMSNMSDQ\nGPYNEYEPTHEGPFIIINGYGQCKCQQLPYKECEV",
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}
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"concentration": 20.0,
"pka": null,
"ph": 7.4,
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},
"purity_method": null,
"name": "Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)",
"ext_coefficient": null,
"contrast": null,
"specific_vol": null,
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"absorbption": null,
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},
"contributor": [
{
"affiliation": [
{
"short_name": "VUB",
"address": "Pleinlaan 2 1050 Brussel ",
"full_name": "Vrije Universiteit Brussel",
"webpage": "http://www.vub.ac.be/"
}
],
"contributor_name": "Alexander",
"contributor_surname": "Shkumatov",
"orcid": null
}
],
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"date": "2015-09-27",
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},
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}
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"experiment_description": "X-ray synchrotron radiation scattering data from solutions of Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct) in 20 mM Tris 150 mM NaCl, 3% glycerol were collected on the ID14-3 beam line at the ESRF storage ring (Grenoble, France) using a 2D Photon counting Pilatus 1M pixel detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Different solute concentrations in the range 1.10-5.50 mg/ml were measured. 10 successive 1 second frames were collected at a sample temperature of 20 degrees centigrade. SAXS data from the samples and corresponding matched solvent blank were normalized to the intensity of the transmitted beam and radially averaged and the scattering of the solvent-blank was subtracted. The low angle data collected were obtained from a merged concentration scattering curve. ",
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"intensities_log_log_plot": "SASDBG3_datloglog_img.png",
"symmetry": null,
"last_modified": "2019-12-06T13:07:15.624532+01:00",
"bragg_peak": []
}查看完整 manifest.json 原文
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