The following content comes directly from the SASBDB entry. Missing values are shown as “—”; SAXSdb does not infer undeclared units.
Every source field is expanded here, including empty values, list members and fields already shown above.
View the complete summary.json source
{
"code": "SASDBV6",
"status": "Published",
"type_of_curve": "Merged",
"angular_unit": "1/A",
"project": {
"title": "Structural and biochemical analysis of <i>Escherichia coli</i> ObgE, a central regulator of bacterial persistence.",
"publication": {
"title": "Structural and biochemical analysis of <i>Escherichia coli</i> ObgE, a central regulator of bacterial persistence.",
"author_list": "Gkekas S, Singh RK, Shkumatov AV, Messens J, Fauvart M, Verstraeten N, Michiels J, Versées W",
"journal": "J Biol Chem",
"doi": "10.1074/jbc.M116.761809",
"pmid": "28223358",
"published_date": "2017 Apr 7"
},
"status": "released",
"submitted_date": "2016-09-28",
"released_date": "2017-02-23"
},
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"experiment": {
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"name": "AVIEX PCCD170170",
"resolution": null
},
"name": "SOLEIL",
"city": "Saint-Aubin",
"country": "France",
"beamline_name": "SWING",
"beam_geometry": "",
"type_of_source": "X-ray synchrotron",
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"sample": {
"molecule": [
{
"long_name": "GTPase ObgE/CgtA",
"short_name": "ObgE_340",
"sequence": "MGSSHHHHHHSSGLVPRGSHMKFVDEASILVVAGDGGNGCVSFRREKYIPKGGPDGGDGGDGGDVWMEADENLNTLIDYR\r\nFEKSFRAERGQNGASRDCTGKRGKDVTIKVPVGTRVIDQGTGETMGDMTKHGQRLLVAKGGWHGLGNTRFKSSVNRTPRQ\r\nKTNGTPGDKRELLLELMLLADVGMLGMPNAGKSTFIRAVSAAKPKVADYPFTTLVPSLGVVRMDNEKSFVVADIPGLIEG\r\nAAEGAGLGIRFLKHLERCRVLLHLIDIDPIDGTDPVENARIIISELELYSQDLATKPRWLVFNKIDLLDKVEAEEKAKAI\r\nAEALGWEDKYYLISAASGLGVKDLCWDVMTFIIENPVA",
"organism": "Escherichia coli",
"uniprot_code": "P42641",
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"oligomerization": "monomer",
"molecular_type": "protein",
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"molecule_source": "biological",
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}
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"comment": null,
"additive": null,
"concentration": null,
"pka": null,
"ph": 7.5,
"deuteration": null
},
"purity_method": null,
"name": "GppNHp bound form of C-terminal deletion mutant of ObgE from E.coli (ObgE_340 with GppNHp)",
"ext_coefficient": null,
"contrast": null,
"specific_vol": null,
"dry_vol": null,
"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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"concentration_unit": null,
"date": "2015-03-12",
"storage_temperature": 10.0,
"cell_temperature": 10.0,
"exposure_time": 2.8,
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"description": "The sample protein includes an N-terminal poly-histidine tag; frames corresponding to the peak in HPLC-SAXS run were averaged using DATAVER v0.2 (r3709)",
"experiment_description": "Synchrotron SAXS data from solutions of the GppNHp bound form of the C-terminal deletion mutant of ObgE from E.coli (ObgE_340 with GppNHp) in 20 mM HEPES, 300 mM NaCl, 250 mM imidazole, 5 mM MgCl2, 2 mM DTT, 400 µM GppNHp, pH 7.5, were collected at the SWING beam line at the SOLEIL Synchrotron (Saint-Aubin, France) using a CCD AVIEX detector at a sample-detector distance of 2.0 m and at a wavelength of λ = 0.103 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). Data collection was performed at at 10°C. 255 successive 2.8 second frames were collected through an HPLC-SEC elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the different curves were scaled for protein concentration, then averaged to produce the final SAXS profile displayed in this entry.",
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"pddf_point_first": null,
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"i0_calibration_standard_data": null,
"intensities_log_log_plot": "SASDBV6_datloglog_img.png",
"symmetry": null,
"last_modified": "2019-12-06T13:07:15.624532+01:00",
"bragg_peak": []
}
View the complete manifest.json source
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