2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
dmax
P(r)
23.0
—
nm
i0
Guinier
111.92
0.102
—
i0
P(r)
112.7
0.09
—
mw
Experimental
240.0
—
kDa
mw
Porod
256.0
—
kDa
porod_volume
Porod
436.03
—
nm³
rg
Guinier
5.98
0.01
nm
rg
P(r)
6.2
0.008
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/f2/sasdcf2/source/SASDCF2.dat
downloaded
50403
full_entry_zip
sasbdb/entries/f2/sasdcf2/source/SASDCF2.zip
downloaded
22936
pddf
sasbdb/entries/f2/sasdcf2/source/SASDCF2.out
downloaded
31267
sascif
sasbdb/entries/f2/sasdcf2/source/SASDCF2.sascif
downloaded
85004
summary
sasbdb/entries/f2/sasdcf2/source/summary.json
downloaded
8502
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5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
Synchrotron SAXS data from solutions of Rab family protein CtRoco L487A (GppNHp) in 20 mM HEPES 150 mM NaCl 5 mM MgCl2 5% Glycerol 1 mM DTT 200µM GppNHp, pH 7.5 were collected on the BM29 camera on the storage ring ESRF (Grenoble, France) using a Pilatus 1M detector at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsin θ/λ and 2θ is the scattering angle). Inline SEC-SAXS was employed at 25°C (50 µl injection volume of an 8 mg/ml protein solution on a Bio SEC-3 HPLC column (Agilent, 3 µm 300 Å)). 41 successive frames were collected through the elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the different curves were scaled and averaged to produce the final SAXS data displayed in this entry.
Related Publication
Title
A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover.
Authors
Deyaert E, Wauters L, Guaitoli G, Konijnenberg A, Leemans M, Terheyden S, Petrovic A, Gallardo R, Nederveen-Schippers LM, Athanasopoulos PS, Pots H, Van Haastert PJM, Sobott F, Gloeckner CJ, Efremov R, Kortholt A, Versées W
DOI / PMID
10.1038/s41467-017-01103-4 / 29044096
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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
SASDCF2
status
Published
type_of_curve
Other
angular_unit
1/nm
project.title
A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover.
project.publication.title
A homologue of the Parkinson's disease-associated protein LRRK2 undergoes a monomer-dimer transition during GTP turnover.
project.publication.author_list
Deyaert E, Wauters L, Guaitoli G, Konijnenberg A, Leemans M, Terheyden S, Petrovic A, Gallardo R, Nederveen-Schippers LM, Athanasopoulos PS, Pots H, Van Haastert PJM, Sobott F, Gloeckner CJ, Efremov R, Kortholt A, Versées W
Synchrotron SAXS data from solutions of Rab family protein CtRoco L487A (GppNHp) in 20 mM HEPES 150 mM NaCl 5 mM MgCl2 5% Glycerol 1 mM DTT 200µM GppNHp, pH 7.5 were collected on the BM29 camera on the storage ring ESRF (Grenoble, France) using a Pilatus 1M detector at a wavelength of λ = 0.099 nm (I(s) vs s, where s = 4πsin θ/λ and 2θ is the scattering angle). Inline SEC-SAXS was employed at 25°C (50 µl injection volume of an 8 mg/ml protein solution on a Bio SEC-3 HPLC column (Agilent, 3 µm 300 Å)). 41 successive frames were collected through the elution peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the different curves were scaled and averaged to produce the final SAXS data displayed in this entry.
