SASBDB entries for UniProt ID:

SASDMG2 – SWAXS data from Lysozyme Solution [Protein concentration 0.4 mg/ml] at 10 °C

UniProt ID: P00698 (19-147) Lysozyme C
Lysozyme C experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.5 nm
Dmax 4.6 nm

SASDMH2 – SAXS Data of Lysozyme (Average of 0.9, 1.8, 2.5 and 5 mg/ml) Analyzed in the q range of 0.08-2.75 1/nm

UniProt ID: P00698 (19-147) Lysozyme C
Lysozyme C experimental SAS data
DAMMIF model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 4.2 nm

SASDMJ2 – SAXS Data of Lysozyme (Average of 0.9, 1.8, 2.5 and 5 mg/ml) Analyzed in the q range of 0.08-4.95 1/nm

UniProt ID: P00698 (19-147) Lysozyme C
Lysozyme C experimental SAS data
DAMMIF model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 4.2 nm

SASDMK2 – SWAXS Data of Lysozyme (Average of 0.9, 1.8, 2.5 and 5 mg/ml) Analyzed in the q range of 0.08-9.9 1/nm

UniProt ID: P00698 (19-147) Lysozyme C
Lysozyme C experimental SAS data
DAMMIF model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 4.2 nm

SASDML2 – SWAXS Data of Lysozyme (Average of 0.9, 1.8, 2.5 and 5 mg/ml) Analyzed in the q range of 0.08-17.2 1/nm

UniProt ID: P00698 (19-147) Lysozyme C
Lysozyme C experimental SAS data
DAMMIF model
Sample: Lysozyme C monomer, 14 kDa Gallus gallus protein
Buffer: 40 mM NaOAc pH 3.8, 150 mM NaCl, pH: 3.8
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 May 2
Visualizing how inclusion of higher reciprocal space in SWAXS data analysis improves shape restoration of biomolecules: case of lysozyme. J Biomol Struct Dyn :1-15 (2021)
Ashish
RgGuinier 1.4 nm
Dmax 4.2 nm

SASDMN2 – Mouse Kirrel2 ectodomain

UniProt ID: Q7TSU7 (21-506) Kin of IRRE-like protein 2
Kin of IRRE-like protein 2 experimental SAS data
Kin of IRRE-like protein 2 Kratky plot
Sample: Kin of IRRE-like protein 2 dimer, 106 kDa Mus musculus protein
Buffer: 10 mM HEPES pH 7.2, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Aug 3
Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors. Cell Rep 37(5):109940 (2021)
Wang J, Vaddadi N, Pak JS, Park Y, Quilez S, Roman CA, Dumontier E, Thornton JW, Cloutier JF, Özkan E
RgGuinier 8.9 nm
Dmax 39.0 nm

SASDMP2 – Mouse Kirrel3 ectodomain

UniProt ID: Q8BR86 (47-517) Kin of IRRE-like protein 3
Kin of IRRE-like protein 3 experimental SAS data
SASREF model
Sample: Kin of IRRE-like protein 3 dimer, 106 kDa Mus musculus protein
Buffer: 10 mM HEPES pH 7.2, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Aug 3
Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors. Cell Rep 37(5):109940 (2021)
Wang J, Vaddadi N, Pak JS, Park Y, Quilez S, Roman CA, Dumontier E, Thornton JW, Cloutier JF, Özkan E
RgGuinier 9.3 nm
Dmax 34.5 nm

SASDMQ2 – Mouse Kirrel3 ectodomain - Q128A mutant

UniProt ID: Q8BR86 (47-517) Kin of IRRE-like protein 3 (Q128A)
Kin of IRRE-like protein 3 (Q128A) experimental SAS data
Mouse Kirrel3 ectodomain - Q128A mutant Rg histogram
Sample: Kin of IRRE-like protein 3 (Q128A) monomer, 53 kDa Mus musculus protein
Buffer: 10 mM HEPES pH 7.2, 150 mM NaCl, pH: 7.2
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2020 Aug 3
Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors. Cell Rep 37(5):109940 (2021)
Wang J, Vaddadi N, Pak JS, Park Y, Quilez S, Roman CA, Dumontier E, Thornton JW, Cloutier JF, Özkan E
RgGuinier 5.4 nm
Dmax 21.3 nm

SASDM43 – RRM1-ZnF1 tandem domains of RNA-binding protein 5 (C191G mutant)

UniProt ID: P52756 (94-210) RNA-binding protein 5 (I107T, C191G)
RNA-binding protein 5 (I107T, C191G) experimental SAS data
Sample: RNA-binding protein 5 (I107T, C191G) monomer, 14 kDa Homo sapiens protein
Buffer: 20 mM MES, 400 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Sep 26
Structural basis for specific RNA recognition by the alternative splicing factor RBM5. Nat Commun 14(1):4233 (2023)
Soni K, Jagtap PKA, Martínez-Lumbreras S, Bonnal S, Geerlof A, Stehle R, Simon B, Valcárcel J, Sattler M
RgGuinier 1.7 nm
Dmax 5.6 nm
VolumePorod 28 nm3

SASDM53 – RRM1-ZnF1-RRM2 triple domains of RNA-binding protein 5 (C191G mutant)

UniProt ID: P52756 (94-315) RNA Binding Motif protein 5 (I107T, C191G)
RNA Binding Motif protein 5 (I107T, C191G) experimental SAS data
RNA Binding Motif protein 5 (I107T, C191G) Kratky plot
Sample: RNA Binding Motif protein 5 (I107T, C191G) monomer, 26 kDa Homo sapiens protein
Buffer: 20 mM MES, 400 mM NaCl, 1 mM DTT, pH: 6.5
Experiment: SAXS data collected at Rigaku BioSAXS-1000, SFB 1035, Technische Universität München on 2017 Feb 9
Structural basis for specific RNA recognition by the alternative splicing factor RBM5. Nat Commun 14(1):4233 (2023)
Soni K, Jagtap PKA, Martínez-Lumbreras S, Bonnal S, Geerlof A, Stehle R, Simon B, Valcárcel J, Sattler M
RgGuinier 2.3 nm
Dmax 7.8 nm
VolumePorod 36 nm3