SASBDB entries for UniProt ID:

SASDB73 – Human dystrophin central domain repeats 4 to 9

UniProt ID: P11532 (718-1368) Dystrophin central domain repeats 4 to 9
Dystrophin central domain repeats 4 to 9 experimental SAS data
NONE model
Sample: Dystrophin central domain repeats 4 to 9 monomer, 76 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 Sep 19
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
Delalande O, Molza AE, Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, Le Rumeur E
RgGuinier 7.7 nm
Dmax 30.5 nm
VolumePorod 123 nm3

SASDB83 – Human dystrophin central domain repeats 16 to 17

UniProt ID: P11532 (1984-2216) Dystrophin central domain repeats 16 to 17.
Dystrophin central domain repeats 16 to 17. experimental SAS data
NONE model
Sample: Dystrophin central domain repeats 16 to 17. monomer, 28 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2012 Sep 19
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
Delalande O, Molza AE, Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, Le Rumeur E
RgGuinier 3.1 nm
Dmax 13.0 nm
VolumePorod 47 nm3

SASDB93 – Human dystrophin central domain repeats 16 to 19

UniProt ID: P11532 (1994-2420) Dystrophin central domain repeats 16 to 19.
Dystrophin central domain repeats 16 to 19. experimental SAS data
NONE model
Sample: Dystrophin central domain repeats 16 to 19. monomer, 50 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol 5% acetonitrile, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2013 Oct 4
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
Delalande O, Molza AE, Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, Le Rumeur E
RgGuinier 4.6 nm
Dmax 20.0 nm
VolumePorod 70 nm3

SASDBA3 – Human dystrophin central domain repeats 20 to 24

UniProt ID: P11532 (2469-3040) Dystrophin central domain repeats 20 to 24.
Dystrophin central domain repeats 20 to 24. experimental SAS data
NONE model
Sample: Dystrophin central domain repeats 20 to 24. monomer, 67 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2011 Jul 10
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
Delalande O, Molza AE, Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, Le Rumeur E
RgGuinier 5.8 nm
Dmax 22.5 nm
VolumePorod 107 nm3

SASDBB3 – Human dystrophin central domain single repeat 23

UniProt ID: P11532 (2800-2939) Dystrophin central domain single repeat 23
Dystrophin central domain single repeat 23 experimental SAS data
NONE model
Sample: Dystrophin central domain single repeat 23 monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM EDTA 2% glycerol, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2011 Oct 7
Dystrophin's central domain forms a complex filament that becomes disorganized by in-frame deletions. J Biol Chem 293(18):6637-6646 (2018)
Delalande O, Molza AE, Dos Santos Morais R, Chéron A, Pollet É, Raguenes-Nicol C, Tascon C, Giudice E, Guilbaud M, Nicolas A, Bondon A, Leturcq F, Férey N, Baaden M, Perez J, Roblin P, Piétri-Rouxel F, Hubert JF, Czjzek M, Le Rumeur E
RgGuinier 2.2 nm
Dmax 7.4 nm
VolumePorod 20 nm3

SASDBG3 – Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)

UniProt ID: Q8BGA3 (30-380) Mouse Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct)
Mouse Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct) experimental SAS data
DAMMIN model
Sample: Mouse Leucine-rich repeat transmembrane neuronal protein 2, cLRRTM2 (stability engineered construct) monomer, 40 kDa Mus musculus protein
Buffer: 20 mM Tris 150 mM NaCl 3% glycerol, pH: 7.4
Experiment: SAXS data collected at ID14-3, ESRF on 2015 Sep 27
Crystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding. Biochemistry 55(6):914-26 (2016)
Paatero A, Rosti K, Shkumatov AV, Sele C, Brunello C, Kysenius K, Singha P, Jokinen V, Huttunen H, Kajander T
RgGuinier 3.3 nm
Dmax 13.1 nm

SASDBH3 – Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 (fragment 30-380)

UniProt ID: Q8BGA3 (30-380) Mouse Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2
Mouse Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 experimental SAS data
DAMMIN model
Sample: Mouse Leucine-rich repeat transmembrane neuronal protein 2, LRRTM2 dimer, 80 kDa Mus musculus protein
Buffer: 20 mM Tris 150 mM NaCl 3% glycerol, pH: 7.4
Experiment: SAXS data collected at ID14-3, ESRF on 2015 Jun 28
Crystal Structure of an Engineered LRRTM2 Synaptic Adhesion Molecule and a Model for Neurexin Binding. Biochemistry 55(6):914-26 (2016)
Paatero A, Rosti K, Shkumatov AV, Sele C, Brunello C, Kysenius K, Singha P, Jokinen V, Huttunen H, Kajander T
RgGuinier 4.2 nm
Dmax 21.6 nm

SASDBJ3 – Bovine serum albumin, monomer from SEC-SAXS

UniProt ID: P02769 (25-607) Bovine serum albumin, monomer
Bovine serum albumin, monomer experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Bovine serum albumin, monomer monomer, 66 kDa Bos taurus protein
Buffer: 25 mM Tris 150 mM NaCl 3% (v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 23
Preparing monodisperse macromolecular samples for successful biological small-angle X-ray and neutron-scattering experiments. Nat Protoc 11(11):2122-2153 (2016)
Jeffries CM, Graewert MA, Blanchet CE, Langley DB, Whitten AE, Svergun DI
RgGuinier 2.8 nm
Dmax 8.2 nm
VolumePorod 100 nm3

SASDBK3 – Bovine serum albumin, dimer from SEC-SAXS

UniProt ID: P02769 (25-607) Bovine serum albumin, dimer
Bovine serum albumin, dimer experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Bovine serum albumin, dimer dimer, 133 kDa Bos taurus protein
Buffer: 25 mM Tris 150 mM NaCl 3% (v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 23
Preparing monodisperse macromolecular samples for successful biological small-angle X-ray and neutron-scattering experiments. Nat Protoc 11(11):2122-2153 (2016)
Jeffries CM, Graewert MA, Blanchet CE, Langley DB, Whitten AE, Svergun DI
RgGuinier 3.9 nm
Dmax 12.7 nm
VolumePorod 202 nm3

SASDBL3 – Highly similar to Actin cross-linking family protein 7 (ACF7) Homo Sapiens

UniProt ID: Q6ZSD7 (1-400) cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7
cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 experimental SAS data
cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Kratky plot
Sample: CDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 monomer, 46 kDa Homo sapiens protein
Buffer: PBS, pH: 7.4
Experiment: SAXS data collected at 12-ID-B SAXS/WAXS, Advanced Photon Source (APS), Argonne National Laboratory on 2014 Nov 10
In vivo epidermal migration requires focal adhesion targeting of ACF7. Nat Commun 7:11692 (2016)
Yue J, Zhang Y, Liang WG, Gou X, Lee P, Liu H, Lyu W, Tang WJ, Chen SY, Yang F, Liang H, Wu X
RgGuinier 3.4 nm
Dmax 13.5 nm
VolumePorod 53 nm3