查看完整 summary.json 原文
{
"code": "SASDC85",
"status": "Published",
"type_of_curve": "Single concentration",
"angular_unit": "1/nm",
"project": {
"title": "Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities.",
"publication": {
"title": "Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities.",
"author_list": "Batista FA, Almeida GS, Seraphim TV, Silva KP, Murta SM, Barbosa LR, Borges JC",
"journal": "FEBS J",
"doi": "10.1111/febs.13141",
"pmid": "25369258",
"published_date": "2015 Jan"
},
"status": "released",
"submitted_date": "2017-06-17",
"released_date": "2017-06-21"
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"contributor": [
{
"affiliation": [
{
"short_name": null,
"address": "São Carlos - SP - Brasil",
"full_name": "Instituto de Química de São Carlos",
"webpage": ""
}
],
"contributor_name": "Júlio",
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"experiment_description": "SAXS experiments were performed at the SAXS2 beam line in the Laboratório Nacional de Luz Síncrotron (LNLS, Campinas-SP, Brazil). The X-ray scattering data (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle; λ = 0.1488 nm) were acquired using a two-dimensional MAR-CCD detector. Measurements were performed with a monochromatic X-ray beam and a sample-to-detector distance of ~1000 mm, corresponding to a scattering vector range of 0.015 < q < 0.35 Å−1. Scattering patterns were recorded at different sample concentrations (approximately 1.0, 2.0 and 4.0 mg/mL) and several frames in order to check for protein aggregation and X-ray damage. No evidence of aggregation or inter-particle interference were observed. The model depicts the averaged spatial representation of the protein (DAMFILT occupancy and volume-corrected bead model).",
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"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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"started_at": "2026-08-11T14:41:37.766817+00:00",
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