2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
dmax
P(r)
25.1
—
nm
i0
Guinier
151.16
0.37
arbitrary
i0
P(r)
152.0
0.1
arbitrary
mw
Experimental
1400.0
—
kDa
mw
Porod
1400.0
—
kDa
porod_volume
Porod
2416.0
—
nm³
rg
Guinier
7.89
0.07
nm
rg
P(r)
7.984
0.07
nm
These values are reported by SASBDB; SAXSdb did not recalculate them from the experimental curve.
▼
3. Source Fits and Models Source Fits & Models
This entry has no source fit record.
▶
4. Source File Index Source Files
Category
Path
Download status
Size
curve
sasbdb/entries/a3/sasdda3/source/SASDDA3.dat
downloaded
13386
full_entry_zip
sasbdb/entries/a3/sasdda3/source/SASDDA3.zip
downloaded
10992
pddf
sasbdb/entries/a3/sasdda3/source/SASDDA3.out
downloaded
23402
sascif
sasbdb/entries/a3/sasdda3/source/SASDDA3.sascif
downloaded
36721
summary
sasbdb/entries/a3/sasdda3/source/summary.json
downloaded
8201
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5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
Synchrotron SAXS data from solutions of ATP-dependent Clp protease ATP-binding subunit ClpC1 (second state) in 50 mM HEPES, pH 7.5, 100 mM KCl, 10% v/v glycerol, 4 mM MgCl2 and 1 mM ATP were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Size-exclusion chromatography SEC-SAXS was performed on a sample at at 20°C. 50 successive 1 second frames were collected through the corresponding SEC elution peak. Each data frame was normalized to the intensity of the transmitted beam and radially averaged (2D- to 1D data reduction). The scattering of the solvent-blank (reduced data obtained from the elution buffer) was subtracted from each sample frame and the resulting subtracted SAXS profiles were scaled and averaged to generate the data displayed in this entry.
Related Publication
Title
The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from <i>Mycobacterium tuberculosis</i>.
Authors
Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda P, Fraga H
DOI / PMID
10.1074/jbc.RA118.002251 / 29632076
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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.
Every source field is expanded here, including empty values, list members and fields already shown above.
summary.json:134 field values
Field path
Raw value
code
SASDDA3
status
Published
type_of_curve
Other
angular_unit
1/nm
project.title
The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from <i>Mycobacterium tuberculosis</i>.
project.publication.title
The antibiotic cyclomarin blocks arginine-phosphate-induced millisecond dynamics in the N-terminal domain of ClpC1 from <i>Mycobacterium tuberculosis</i>.
project.publication.author_list
Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda P, Fraga H
European Molecular Biology Laboratory (EMBL) - Grenoble Outstation
experiment.contributor[0].affiliation[0].webpage
https://www.embl.fr/
experiment.contributor[0].contributor_name
Martha
experiment.contributor[0].contributor_surname
Brennich
experiment.contributor[0].orcid
null
experiment.concentration_method
null
experiment.concentration_unit
null
experiment.date
2017-09-18
experiment.storage_temperature
20.0
experiment.cell_temperature
20.0
experiment.exposure_time
1.0
experiment.number_of_frames
50
experiment.wavelength
0.099
experiment.sample_detector_distance
2.867
experiment.concentration_min
null
experiment.concentration_max
null
experiment.sample_volume
null
experiment.flow_rate
null
experiment.s_min
0.095
experiment.s_max
1.443
experiment.total_exposure_time
null
experiment.seccolumn
null
fits
[]
estimated_volume_method
null
pddf_software
ATSAS GNOM
pddf_software_version
5.0
i0_calibration_standard
null
description
null
experiment_description
Synchrotron SAXS data from solutions of ATP-dependent Clp protease ATP-binding subunit ClpC1 (second state) in 50 mM HEPES, pH 7.5, 100 mM KCl, 10% v/v glycerol, 4 mM MgCl2 and 1 mM ATP were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Size-exclusion chromatography SEC-SAXS was performed on a sample at at 20°C. 50 successive 1 second frames were collected through the corresponding SEC elution peak. Each data frame was normalized to the intensity of the transmitted beam and radially averaged (2D- to 1D data reduction). The scattering of the solvent-blank (reduced data obtained from the elution buffer) was subtracted from each sample frame and the resulting subtracted SAXS profiles were scaled and averaged to generate the data displayed in this entry.