SASBDB entries for UniProt ID:

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

SASDBN3 – Highly similar to Actin cross-linking family protein 7 (ACF7) Y259D mutant Homo Sapiens

UniProt ID: Q6ZSD7 (1-400) cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Y259D mutant
cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Y259D mutant experimental SAS data
cDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Y259D mutant Kratky plot
Sample: CDNA FLJ45612 fis, clone BRTHA3025073, highly similar to Actin cross-linking family protein 7 Y259D mutant 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 7
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 55 nm3

SASDBQ3 – Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164)

UniProt ID: T2B9R0 (1-164) Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164)
Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164) experimental SAS data
DAMMIF model
Sample: Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164) monomer, 18 kDa Middle East respiratory … protein
Buffer: 10 mM HEPES 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2015 Oct 5
Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering. Acta Crystallogr D Struct Biol 72(Pt 2):192-202 (2016)
Papageorgiou N, Lichière J, Baklouti A, Ferron F, Sévajol M, Canard B, Coutard B
RgGuinier 2.0 nm
Dmax 8.0 nm
VolumePorod 28 nm3

SASDBR3 – Wild type RNF8 complexed with Ubc13 (C87K, K92A mutant): conjugated to Ubiquitin

UniProt ID: O76064 (345-485) E3 ubiquitin-protein ligase RNF8

UniProt ID: P61088 (1-152) Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)

UniProt ID: P0CG48 (1-76) Polyubiquitin-C
E3 ubiquitin-protein ligase RNF8Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)Polyubiquitin-C experimental SAS data
MES-FOXS model
Sample: E3 ubiquitin-protein ligase RNF8 dimer, 35 kDa Homo sapiens protein
Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A) dimer, 36 kDa Homo sapiens protein
Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
Buffer: 20 mM HEPES 200 mM NaCl 0.01 mM ZnSO4 1 mM DTT, pH: 6.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Sep 8
RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment. J Biol Chem 291(18):9396-410 (2016)
Hodge CD, Ismail IH, Edwards RA, Hura GL, Xiao AT, Tainer JA, Hendzel MJ, Glover JN
RgGuinier 4.5 nm
Dmax 18.9 nm
VolumePorod 119 nm3

SASDBS3 – Wild type RNF8 complexed with Ubc13 (C87K, K92A mutant) and Mms2: conjugated to Ubiquitin

UniProt ID: O76064 (345-485) E3 ubiquitin-protein ligase RNF8

UniProt ID: P61088 (1-152) Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)

UniProt ID: P0CG48 (1-76) Polyubiquitin-C

UniProt ID: Q15819 (1-145) Ubiquitin-conjugating enzyme E2 variant 2
E3 ubiquitin-protein ligase RNF8Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)Polyubiquitin-CUbiquitin-conjugating enzyme E2 variant 2 experimental SAS data
MES-FOXS model
Sample: E3 ubiquitin-protein ligase RNF8 dimer, 35 kDa Homo sapiens protein
Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A) dimer, 36 kDa Homo sapiens protein
Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
Ubiquitin-conjugating enzyme E2 variant 2 dimer, 34 kDa Homo sapiens protein
Buffer: 20 mM HEPES 200 mM NaCl 0.01 mM ZnSO4 1 mM DTT, pH: 6.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Sep 8
RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment. J Biol Chem 291(18):9396-410 (2016)
Hodge CD, Ismail IH, Edwards RA, Hura GL, Xiao AT, Tainer JA, Hendzel MJ, Glover JN
RgGuinier 5.4 nm
Dmax 23.8 nm
VolumePorod 214 nm3

SASDBT3 – RNF8 (L451D mutant) complexed with Ubc13 (C87K, K92A mutant): conjugated to Ubiquitin

UniProt ID: P61088 (1-152) Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)

UniProt ID: P0CG48 (1-76) Polyubiquitin-C

UniProt ID: O76064 (345-485) E3 ubiquitin-protein ligase RNF8 mutant (L451D)
Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)Polyubiquitin-CE3 ubiquitin-protein ligase RNF8 mutant (L451D) experimental SAS data
MES-FOXS model
Sample: Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A) dimer, 36 kDa Homo sapiens protein
Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
E3 ubiquitin-protein ligase RNF8 mutant (L451D) dimer, 35 kDa Homo sapiens protein
Buffer: 20 mM HEPES 200 mM NaCl 0.01 mM ZnSO4 1 mM DTT, pH: 6.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Sep 8
RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment. J Biol Chem 291(18):9396-410 (2016)
Hodge CD, Ismail IH, Edwards RA, Hura GL, Xiao AT, Tainer JA, Hendzel MJ, Glover JN
RgGuinier 4.3 nm
Dmax 18.9 nm
VolumePorod 111 nm3

SASDBU3 – RNF8 (L451D mutant) complexed with Ubc13 (C87K, K92A mutant) and Mms2: conjugated to Ubiquitin

UniProt ID: P61088 (1-152) Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)

UniProt ID: P0CG48 (1-76) Polyubiquitin-C

UniProt ID: Q15819 (1-145) Ubiquitin-conjugating enzyme E2 variant 2

UniProt ID: O76064 (345-485) E3 ubiquitin-protein ligase RNF8 mutant (L451D)
Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A)Polyubiquitin-CUbiquitin-conjugating enzyme E2 variant 2E3 ubiquitin-protein ligase RNF8 mutant (L451D) experimental SAS data
MES-FOXS model
Sample: Ubiquitin-conjugating enzyme E2 N double mutant (C87K, K92A) dimer, 36 kDa Homo sapiens protein
Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
Ubiquitin-conjugating enzyme E2 variant 2 dimer, 34 kDa Homo sapiens protein
E3 ubiquitin-protein ligase RNF8 mutant (L451D) dimer, 35 kDa Homo sapiens protein
Buffer: 20 mM HEPES 200 mM NaCl 0.01 mM ZnSO4 1 mM DTT, pH: 6.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Sep 8
RNF8 E3 Ubiquitin Ligase Stimulates Ubc13 E2 Conjugating Activity That Is Essential for DNA Double Strand Break Signaling and BRCA1 Tumor Suppressor Recruitment. J Biol Chem 291(18):9396-410 (2016)
Hodge CD, Ismail IH, Edwards RA, Hura GL, Xiao AT, Tainer JA, Hendzel MJ, Glover JN
RgGuinier 5.2 nm
Dmax 23.8 nm
VolumePorod 192 nm3

SASDBV3 – Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant)

UniProt ID: P11532 (1991-2694) Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47)
Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47) experimental SAS data
GASBOR model
Sample: Dystrophin central domain repeats 16 to 21 (Δ2146-2305; Becker muscular dystrophy variant, deletion of exons 45-47) monomer, 64 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 2014 Feb 5
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 6.0 nm
Dmax 21.0 nm
VolumePorod 184 nm3