2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
dmax
P(r)
20.0
—
nm
i0
Guinier
126992.0
52.0
arbitrary
i0
P(r)
128200.0
—
arbitrary
mw
Experimental
420.0
—
kDa
mw
Porod
415.0
—
kDa
porod_volume
Porod
666.0
—
nm³
rg
Guinier
6.12
0.02
nm
rg
P(r)
6.269
—
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/66/sasde66/source/SASDE66.dat
downloaded
85274
full_entry_zip
sasbdb/entries/66/sasde66/source/SASDE66.zip
downloaded
36189
pddf
sasbdb/entries/66/sasde66/source/SASDE66.out
downloaded
45519
sascif
sasbdb/entries/66/sasde66/source/SASDE66.sascif
downloaded
135525
summary
sasbdb/entries/66/sasde66/source/summary.json
downloaded
7175
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5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
Synchrotron SAXS data from solutions of C. limicola acetyl citrate lyase (ACL) in 20mM HEPES, 150mM NaCl, pH 7.2 were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Size-exclusion chromatography SAXS (SEC-SAXS) was employed using a sample injection concentration of 17.50 mg/ml. Data were measured at through the SEC elution at 20°C. 900 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of an appropriate solvent-blank was subtracted using the CHROMIXS SEC-SAXS analysis package.
Related Publication
Title
Structure of ATP citrate lyase and the origin of citrate synthase in the Krebs cycle.
Authors
Verschueren KHG, Blanchet C, Felix J, Dansercoer A, De Vos D, Bloch Y, Van Beeumen J, Svergun D, Gutsche I, Savvides SN, Verstraete K
DOI / PMID
10.1038/s41586-019-1095-5 / 30944476
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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.
European Molecular Biology Laboratory (EMBL) - Hamburg outstation
experiment.contributor[0].affiliation[0].webpage
http://www.embl-hamburg.de/index.php
experiment.contributor[0].contributor_name
Clement
experiment.contributor[0].contributor_surname
Blanchet
experiment.contributor[0].orcid
null
experiment.concentration_method
null
experiment.concentration_unit
null
experiment.date
2017-09-04
experiment.storage_temperature
20.0
experiment.cell_temperature
20.0
experiment.exposure_time
1.0
experiment.number_of_frames
900
experiment.wavelength
0.124
experiment.sample_detector_distance
3.1
experiment.concentration_min
null
experiment.concentration_max
17.5
experiment.sample_volume
null
experiment.flow_rate
null
experiment.s_min
0.025
experiment.s_max
5.064
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 C. limicola acetyl citrate lyase (ACL) in 20mM HEPES, 150mM NaCl, pH 7.2 were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3.1 m and at a wavelength of λ = 0.124 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Size-exclusion chromatography SAXS (SEC-SAXS) was employed using a sample injection concentration of 17.50 mg/ml. Data were measured at through the SEC elution at 20°C. 900 successive 1 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of an appropriate solvent-blank was subtracted using the CHROMIXS SEC-SAXS analysis package.