2. Measurements Reported by SASBDB Reported Results
Metric
Method
Value
Uncertainty
Unit
dmax
P(r)
7.32
—
Å
i0
Guinier
60.86
0.38
arbitrary
i0
P(r)
63.84
0.19
arbitrary
mw
Experimental
73.7
—
kDa
mw
Porod
65.0
—
kDa
porod_volume
Porod
104.0
—
ų
rg
Guinier
2.421
0.018
Å
rg
P(r)
2.525
0.005
Å
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.
▶
4. Source File Index Source Files
Category
Path
Download status
Size
curve
sasbdb/entries/m4/sasddm4/source/SASDDM4.dat
downloaded
43797
full_entry_zip
sasbdb/entries/m4/sasddm4/source/SASDDM4.zip
downloaded
39526
pddf
sasbdb/entries/m4/sasddm4/source/SASDDM4.out
downloaded
83455
sascif
sasbdb/entries/m4/sasddm4/source/SASDDM4.sascif
downloaded
103391
summary
sasbdb/entries/m4/sasddm4/source/summary.json
downloaded
5976
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5. Experiment Description and Publication Experiment & Publication
Related Publication
Title
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.
Authors
Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D
DOI / PMID
10.1016/j.abb.2018.06.010 / 29940152
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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
SASDDM4
status
Published
type_of_curve
Single concentration
angular_unit
1/A
project.title
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.
project.publication.title
Crystal structure of the flavin reductase of Acinetobacter baumannii p-hydroxyphenylacetate 3-hydroxylase (HPAH) and identification of amino acid residues underlying its regulation by aromatic ligands.
project.publication.author_list
Yuenyao A, Petchyam N, Kamonsutthipaijit N, Chaiyen P, Pakotiprapha D