SASBDB entries for UniProt ID:

SASDD69 – Medium 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 3.8 nm
VolumePorod 275 nm3

SASDD79 – High 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 3.8 nm
VolumePorod 277 nm3

SASDD89 – Structure of Halobacterium salinarum VNG0258H/RosR in the presence of 2 M KCl

UniProt ID: Q9HSF4 (1-116) VNG0258H/RosR
VNG0258H/RosR experimental SAS data
DAMMIN model
Sample: VNG0258H/RosR dimer, 29 kDa Halobacterium salinarum NRC-1 protein
Buffer: 50 mM HEPES, 2 M KCl, 0.02% NaN3, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Mar 7
The 3-D structure of VNG0258H/RosR - A haloarchaeal DNA-binding protein in its ionic shell. J Struct Biol (2018)
Kutnowski N, Shmuely H, Dahan I, Shmulevich F, Davidov G, Shahar A, Eichler J, Zarivach R, Shaanan B
RgGuinier 2.3 nm
Dmax 7.5 nm
VolumePorod 58 nm3

SASDD99 – Structure of Halobacterium salinarum VNG0258H/RosR in the presence of 2 M NaCl

UniProt ID: Q9HSF4 (1-116) VNG0258H/RosR
VNG0258H/RosR experimental SAS data
DAMMIN model
Sample: VNG0258H/RosR dimer, 29 kDa Halobacterium salinarum NRC-1 protein
Buffer: 50 mM HEPES, 2 M NaCl, 0.02% NaN3, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Mar 7
The 3-D structure of VNG0258H/RosR - A haloarchaeal DNA-binding protein in its ionic shell. J Struct Biol (2018)
Kutnowski N, Shmuely H, Dahan I, Shmulevich F, Davidov G, Shahar A, Eichler J, Zarivach R, Shaanan B
RgGuinier 2.4 nm
Dmax 7.7 nm
VolumePorod 63 nm3

SASDDA9 – Structure of Halobacterium salinarum VNG0258H/RosR in the presence of 2 M KBr

UniProt ID: Q9HSF4 (None-None) VNG0258H/RosR
VNG0258H/RosR experimental SAS data
DAMMIN model
Sample: VNG0258H/RosR dimer, 29 kDa Halobacterium salinarum NRC-1 protein
Buffer: 50 mM HEPES, 2 M KBr, 0.02% NaN3, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Mar 7
The 3-D structure of VNG0258H/RosR - A haloarchaeal DNA-binding protein in its ionic shell. J Struct Biol (2018)
Kutnowski N, Shmuely H, Dahan I, Shmulevich F, Davidov G, Shahar A, Eichler J, Zarivach R, Shaanan B
RgGuinier 2.3 nm
Dmax 7.7 nm
VolumePorod 46 nm3

SASDDB9 – Structure of Halobacterium salinarum VNG0258H/RosR in the presence of 2 M NaBr

UniProt ID: Q9HSF4 (1-116) VNG0258H/RosR
VNG0258H/RosR experimental SAS data
DAMMIN model
Sample: VNG0258H/RosR dimer, 29 kDa Halobacterium salinarum NRC-1 protein
Buffer: 50 mM HEPES, 2 M NaBr, 0.02% NaN3, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Sep 26
The 3-D structure of VNG0258H/RosR - A haloarchaeal DNA-binding protein in its ionic shell. J Struct Biol (2018)
Kutnowski N, Shmuely H, Dahan I, Shmulevich F, Davidov G, Shahar A, Eichler J, Zarivach R, Shaanan B
RgGuinier 2.5 nm
Dmax 8.1 nm
VolumePorod 59 nm3

SASDDC9 – Structure of Halobacterium salinarum VNG0258H/RosR in the presence of 2 M RbCl

UniProt ID: Q9HSF4 (1-116) VNG0258H/RosR
VNG0258H/RosR experimental SAS data
DAMMIN model
Sample: VNG0258H/RosR dimer, 29 kDa Halobacterium salinarum NRC-1 protein
Buffer: 50 mM HEPES, 2 M RbCl, 0.02% NaN3, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Mar 7
The 3-D structure of VNG0258H/RosR - A haloarchaeal DNA-binding protein in its ionic shell. J Struct Biol (2018)
Kutnowski N, Shmuely H, Dahan I, Shmulevich F, Davidov G, Shahar A, Eichler J, Zarivach R, Shaanan B
RgGuinier 3.3 nm
Dmax 9.3 nm
VolumePorod 89 nm3

SASDDD9 – Cardiac myosin binding protein C: tri-helix bundle from the motif with C2 domain

UniProt ID: Q14896 (319-451) cardiac myosin binding protein C: tri-helix bundle-C2
cardiac myosin binding protein C: tri-helix bundle-C2 experimental SAS data
Cardiac myosin binding protein C: tri-helix bundle from the motif with C2 domain Rg histogram
Sample: Cardiac myosin binding protein C: tri-helix bundle-C2 monomer, 15 kDa human sequence obtained … protein
Buffer: 150 mM NaCl, 10 mM MES, 2 mM TCEP, 1 mM NaN3 at 4°C, pH: 6.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Apr 18
A Highly Conserved Yet Flexible Linker Is Part of a Polymorphic Protein-Binding Domain in Myosin-Binding Protein C. Structure 24(11):2000-2007 (2016)
Michie KA, Kwan AH, Tung CS, Guss JM, Trewhella J
RgGuinier 1.9 nm
Dmax 8.0 nm
VolumePorod 20 nm3

SASDDE9 – Synechocystis fluorescence recovery protein FRPcc in the pre-oxidized state (CC mutant)

UniProt ID: P74103 (None-None) Fluorescence recovery protein
Fluorescence recovery protein experimental SAS data
CORAL model
Sample: Fluorescence recovery protein dimer, 28 kDa Synechocystis sp. PCC … protein
Buffer: 20 mM Tris, 150 mM NaCl, 3% glycerol, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 1
OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria. Nat Commun 9(1):3869 (2018)
Sluchanko NN, Slonimskiy YB, Shirshin EA, Moldenhauer M, Friedrich T, Maksimov EG
RgGuinier 2.9 nm
Dmax 13.0 nm
VolumePorod 43 nm3

SASDDF9 – Synechocystis orange carotenoid-binding protein devoid of the NTE (OCP-ΔNTE, orange form)

UniProt ID: P74102 (None-None) Orange carotenoid-binding protein
Orange carotenoid-binding protein experimental SAS data
CORAL model
Sample: Orange carotenoid-binding protein monomer, 34 kDa Synechocystis sp. PCC … protein
Buffer: 20 mM Tris, 150 mM NaCl, 3% glycerol, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 1
OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria. Nat Commun 9(1):3869 (2018)
Sluchanko NN, Slonimskiy YB, Shirshin EA, Moldenhauer M, Friedrich T, Maksimov EG
RgGuinier 2.2 nm
Dmax 7.4 nm
VolumePorod 57 nm3