Open Dataset XSAKDRGZ
SEC-SAXS-MALS for mAb1 ( SinoBiological: 40143-MM05) against the N-terminal domain of nucleocapsid protein from SARS-CoV-2
We conducted a structural characterization of mAbs against the N-terminal domain of nucleocapsid protein (NPNTD) from SARS-CoV-2 using small-angle X-ray scattering (SAXS). Our solution-based results distinguished the mAbs’ flexibility and how this flexibility impacts the assembly of multiple mAbs on an antigen. By pairing two mAbs that bind different epitopes on the NPNTD, we show that flexible mAbs form a closed sandwich-like complex. With rigid mAbs, a juxtaposition of the Fabs is prevented, enforcing a linear arrangement of the mAb pair, which facilitates further mAb polymerization.
Experimental descriptionFor SEC-MALS-SAXS experiments, 60 uL of a sample containing mAb1 ~1.5 mg/mL was prepared in PBS pH 7.4 buffer. SEC-MALS-SAXS was collected at the SIBYLS beamline (BL 12.3.1) at the Advanced Light Source (ALS) at Lawrence Berkeley National Laboratory (LBNL) in Berkeley, California.
File description*cbf.dat > unsubtracted SAXS curves for 600 two-second exposures across the SEC elution profile. *.dat > final merged SAXS profile for main SEC peak *.pdb > two multistate atomic model *.pdf > SEC-MALS results
2021-03-04
Published2021-05-21
Data collection techniqueSEC-SAXS
Journal DOI
Beamline
Wavelength
Sample to Detector Distance
Michal Hammel
Lawrence Berkeley National Laboratory, The SIBYLS Beamline
United States of America
Collaborators
https://www.biorxiv.org/content/10.1101/2021.01.13.426597v1
Project LeaderMichal Hammel
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Complete Set of SAS Data Files
The complete SAS dataset is downloadable as a zip file.
- mAb1.zip Download
Individual SAS Data Files (total 1)
These are individual SAS data files that may be raw or processed (merged, etc.). These may or not be included in a zip file containing a larger dataset.
- ant1.dat Download
Supplemental Data and Supporting Materials (total 0)
These data and materials may include X-ray crystal structure coordinates, multi-angle light scattering data, .etc. It may also include additional details or methods pertaining to the SAXS experiments, or the researcher's interpretations of the results.
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SAXS Similarity SAXS FrameSlice