SASBDB entries for UniProt ID:

SASDDT8 – Neural/ectodermal development factor IMP-L2 in complex with insulin-like peptide 5 (DILP5)

UniProt ID: E7BBS4 (None-None) Insulin-like peptide 5

UniProt ID: Q09024 (None-None) Neural/ectodermal development factor IMP-L2
Insulin-like peptide 5Neural/ectodermal development factor IMP-L2 experimental SAS data
Insulin-like peptide 5 Neural/ectodermal development factor IMP-L2 Kratky plot
Sample: Insulin-like peptide 5 monomer, 5 kDa Drosophila melanogaster protein
Neural/ectodermal development factor IMP-L2 monomer, 30 kDa Drosophila melanogaster protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at ID14-3, ESRF on 2011 Nov 20
Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones. Nat Commun 9(1):3860 (2018)
Roed NK, Viola CM, Kristensen O, Schluckebier G, Norrman M, Sajid W, Wade JD, Andersen AS, Kristensen C, Ganderton TR, Turkenburg JP, De Meyts P, Brzozowski AM
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 55 nm3

SASDDU8 – Multidomain architecture of the estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains

UniProt ID: P03372 (181-552) Estrogen receptor

UniProt ID: None (None-None) ERE1

UniProt ID: None (None-None) ERE2

UniProt ID: None (None-None) Estradiol

UniProt ID: None (None-None) hERa peptide1

UniProt ID: None (None-None) hERa peptide2
Estrogen receptorERE1ERE2EstradiolhERa peptide1hERa peptide2 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Estrogen receptor dimer, 85 kDa protein
ERE1 monomer, 6 kDa Homo sapiens DNA
ERE2 monomer, 6 kDa Homo sapiens DNA
Estradiol dimer, 0 kDa
HERa peptide1 monomer, 2 kDa protein
HERa peptide2 monomer, 2 kDa protein
Buffer: 10 mM CHES (pH9.5), 125 mM NaCl, 5mM KCl, 4 mM MgCl2, 50 mM arginine, 50 mM glutamate, 5 mM TCEP, 5% glycerol, 10 µm Zn acetate, 10 µM estradiol, pH: 9.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Aug 10
Multidomain architecture of estrogen receptor reveals interfacial cross-talk between its DNA-binding and ligand-binding domains. Nat Commun 9(1):3520 (2018)
Huang W, Peng Y, Kiselar J, Zhao X, Albaqami A, Mendez D, Chen Y, Chakravarthy S, Gupta S, Ralston C, Kao HY, Chance MR, Yang S
RgGuinier 3.8 nm
Dmax 11.5 nm

SASDDV8 – Boiled chicken egg albumen

UniProt ID: P01012 (None-None) Ovalbumin
Ovalbumin experimental SAS data
Ovalbumin Kratky plot
Sample: Ovalbumin monomer, 43 kDa Gallus gallus protein
Buffer: Water, pH: 7
Experiment: SAXS data collected at Bruker Nonius FR591, University of Pennslyvania on 2013 Jun 27
The Proof Is in the Pidan: Generalizing Proteins as Patchy Particles. ACS Cent Sci 4(7):840-853 (2018)
Cai J, Sweeney AM

SASDDW8 – Chinese century egg albumen (pidan) made from quail egg

UniProt ID: Q6V115 (None-None) Ovalbumin (common quail)
Ovalbumin (common quail) experimental SAS data
Ovalbumin (common quail) Kratky plot
Sample: Ovalbumin (common quail) monomer, 42 kDa Coturnix coturnix protein
Buffer: Water, pH: 7
Experiment: SAXS data collected at Bruker Nonius FR591, University of Pennslyvania on 2013 Jun 27
The Proof Is in the Pidan: Generalizing Proteins as Patchy Particles. ACS Cent Sci 4(7):840-853 (2018)
Cai J, Sweeney AM

SASDDX8 – Raw chicken egg albumen

UniProt ID: P01012 (None-None) Ovalbumin
Ovalbumin experimental SAS data
Ovalbumin Kratky plot
Sample: Ovalbumin monomer, 43 kDa Gallus gallus protein
Buffer: Water, pH: 7
Experiment: SAXS data collected at Bruker Nonius FR591, University of Pennslyvania on 2013 Jun 27
The Proof Is in the Pidan: Generalizing Proteins as Patchy Particles. ACS Cent Sci 4(7):840-853 (2018)
Cai J, Sweeney AM

SASDDY8 – Chicken ovalbumin gel at high pH

UniProt ID: P01012 (None-None) Ovalbumin
Ovalbumin experimental SAS data
DAMMIF model
Sample: Ovalbumin monomer, 43 kDa Gallus gallus protein
Buffer: 0.16 M NaOH, pH: 13.2
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 Feb 21
The Proof Is in the Pidan: Generalizing Proteins as Patchy Particles. ACS Cent Sci 4(7):840-853 (2018)
Cai J, Sweeney AM

SASDD29 – Low load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS

UniProt ID: P49419 (None-None) Alpha-aminoadipic semialdehyde dehydrogenase
Alpha-aminoadipic semialdehyde dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Feb 22
NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1. FEBS Lett (2018)
Korasick DA, White TA, Chakravarthy S, Tanner JJ
RgGuinier 3.5 nm
VolumePorod 212 nm3

SASDD39 – Medium load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS

UniProt ID: P49419 (None-None) Alpha-aminoadipic semialdehyde dehydrogenase
Alpha-aminoadipic semialdehyde dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Feb 22
NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1. FEBS Lett (2018)
Korasick DA, White TA, Chakravarthy S, Tanner JJ
RgGuinier 3.7 nm
VolumePorod 229 nm3

SASDD49 – High load concentration of apo alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) collected by SEC-SAXS

UniProt ID: P49419 (None-None) Alpha-aminoadipic semialdehyde dehydrogenase
Alpha-aminoadipic semialdehyde dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Feb 22
NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1. FEBS Lett (2018)
Korasick DA, White TA, Chakravarthy S, Tanner JJ
RgGuinier 3.7 nm
VolumePorod 238 nm3

SASDD59 – Low load concentration of alpha-aminoadipic semialdehyde dehydrogenase (ALDH7A1) with nicotinamide adenine dinucleotide (NAD) collected by SEC-SAXS

UniProt ID: P49419 (None-None) Alpha-aminoadipic semialdehyde dehydrogenase
Alpha-aminoadipic semialdehyde dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Alpha-aminoadipic semialdehyde dehydrogenase tetramer, 222 kDa Homo sapiens protein
Buffer: 50 mM Tris, 50 mM NaCl, 0.5 mM DTT, 5% (v/v) glycerol, 1 mM NAD, pH: 7.8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Feb 22
NAD+ Promotes Assembly of the Active Tetramer of Aldehyde Dehydrogenase 7A1. FEBS Lett (2018)
Korasick DA, White TA, Chakravarthy S, Tanner JJ
RgGuinier 3.7 nm
VolumePorod 277 nm3