2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
dmax
P(r)
6.17
—
nm
i0
Guinier
0.00893092
—
1/cm
i0
P(r)
0.008933
—
1/cm
mw
Experimental
13.69
—
kDa
mw
Porod
17.7
—
kDa
porod_volume
Porod
28.34
—
nm³
rg
Guinier
1.65
0.004
nm
rg
P(r)
1.672
—
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/w3/sasdww3/source/SASDWW3.dat
downloaded
62214
full_entry_zip
sasbdb/entries/w3/sasdww3/source/SASDWW3.zip
downloaded
43246
pddf
sasbdb/entries/w3/sasdww3/source/SASDWW3.out
downloaded
113609
sascif
sasbdb/entries/w3/sasdww3/source/SASDWW3.sascif
not_available
—
summary
sasbdb/entries/w3/sasdww3/source/summary.json
downloaded
6791
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5. Experiment Description and Publication Experiment & Publication
Original Experiment Description
Synchrotron SAXS data from solutions of crTPpart2 of CysK in 20 mM HEPES, 300 mM NaCl, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.7 and 10.6 mg/ml were measured at 10°C. 40 successive 0.095 second 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.
Related Publication
Title
The <i>Paulinella</i>
chromatophore transit peptide part2 adopts a structural fold similar to the γ-glutamyl-cyclotransferase fold
Authors
Klimenko V, Reiners J, Applegate V, Reimann K, Popowicz G, Hoeppner A, Papadopoulos A, Smits S, Nowack E
DOI / PMID
10.1093/plphys/kiaf504 / —
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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.
No UniProt ID is available. This sequence was derived from the transcripts (GenBank: GEZN00000000.1, Nowack, E. C. M., Price, D. C., Bhattacharya, D., Singer, A., Melkonian, M. and Grossman, A. R. (2016) Gene transfers from diverse bacteria compensate for reductive genome evolution in the chromatophore of Paulinella chromatophora. Proc. Nati. Acad. Sci. USA, 113, 12214-12219.) Scaffold4337-size1989, encoding a protein annotated as cysteine synthase A (CysK).
Synchrotron SAXS data from solutions of crTPpart2 of CysK in 20 mM HEPES, 300 mM NaCl, pH 8 were collected on the EMBL P12 beam line at PETRA III (DESY; Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.7 and 10.6 mg/ml were measured at 10°C. 40 successive 0.095 second 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. The low angle data collected at lower concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.