2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
i0
Guinier
63.72
0.25
—
mw
Experimental
66.0
—
kDa
rg
Guinier
8.29
0.4
nm
These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.
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3. Source Fits and Models Source Fits & Models
This entry has no source fit record.
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4. Source File Index Source Files
Category
Path
Download status
Size
curve
sasbdb/entries/62/sasdd62/source/SASDD62.dat
downloaded
57604
full_entry_zip
sasbdb/entries/62/sasdd62/source/SASDD62.zip
downloaded
17558
pddf
sasbdb/entries/62/sasdd62/source/SASDD62.out
not_listed
—
sascif
sasbdb/entries/62/sasdd62/source/SASDD62.sascif
downloaded
62196
summary
sasbdb/entries/62/sasdd62/source/summary.json
downloaded
8313
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5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
Synchrotron SAXS data from solutions of microtubule associated protein MAP2c (isoform 3) in 50 mM MOPS, 150 mM NaCl, 0,03% NaN3, pH 6.9 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at an X-ray wavelength, λ, of 0.099 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). One solute concentration of 12.00 mg/ml was measured at 20°C. A total of 10 successive 1 s data 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 and the data were scaled for protein concentration.
Related Publication
Title
Functionally specific binding regions of microtubule-associated protein 2c exhibit distinct conformations and dynamics.
Authors
Melková K, Zapletal V, Jansen S, Nomilner E, Zachrdla M, Hritz J, Nováček J, Zweckstetter M, Jensen MR, Blackledge M, Žídek L
DOI / PMID
10.1074/jbc.RA118.001769 / 29925592
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6. Complete Source Record Complete Source Record
The following content comes directly from the SASBDB entry. Missing values are shown as “—”; SAXSdb does not infer undeclared units.
Masaryk University; Research group Structure and Dynamics of Proteins.
experiment.contributor[0].affiliation[0].webpage
https://www.muni.cz/
experiment.contributor[0].contributor_name
Vojtech
experiment.contributor[0].contributor_surname
Zapletal
experiment.contributor[0].orcid
null
experiment.concentration_method
null
experiment.concentration_unit
null
experiment.date
2017-04-21
experiment.storage_temperature
20.0
experiment.cell_temperature
20.0
experiment.exposure_time
1.0
experiment.number_of_frames
10
experiment.wavelength
0.099
experiment.sample_detector_distance
null
experiment.concentration_min
null
experiment.concentration_max
12.0
experiment.sample_volume
null
experiment.flow_rate
null
experiment.s_min
0.031
experiment.s_max
4.944
experiment.total_exposure_time
null
experiment.seccolumn
null
fits
[]
estimated_volume_method
null
pddf_software
null
pddf_software_version
null
i0_calibration_standard
null
description
null
experiment_description
Synchrotron SAXS data from solutions of microtubule associated protein MAP2c (isoform 3) in 50 mM MOPS, 150 mM NaCl, 0,03% NaN3, pH 6.9 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at an X-ray wavelength, λ, of 0.099 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). One solute concentration of 12.00 mg/ml was measured at 20°C. A total of 10 successive 1 s data 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 and the data were scaled for protein concentration.