SASBDB entries for UniProt ID:

SASDNR3 – Fibrillin-1 fragment PF3

UniProt ID: P35555 (1-722) Fibrillin-1 PF3
Fibrillin-1 PF3 experimental SAS data
DAMMIF model
Sample: Fibrillin-1 PF3 monomer, 78 kDa Homo sapiens protein
Buffer: Tris buffered saline, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 12
Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation. Matrix Biol (2022)
Lockhart-Cairns MP, Cain SA, Dajani R, Steer R, Thomson J, Alanazi YF, Kielty CM, Baldock C
RgGuinier 5.4 nm
Dmax 24.0 nm
VolumePorod 141 nm3

SASDNS3 – Latent-transforming growth factor beta-binding protein 1 C-terminus

UniProt ID: Q14766-2 (1329-1721) Latent-transforming growth factor beta-binding protein 1
Latent-transforming growth factor beta-binding protein 1 experimental SAS data
DAMMIF model
Sample: Latent-transforming growth factor beta-binding protein 1 monomer, 44 kDa Homo sapiens protein
Buffer: Tris buffered saline, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Dec 12
Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation. Matrix Biol (2022)
Lockhart-Cairns MP, Cain SA, Dajani R, Steer R, Thomson J, Alanazi YF, Kielty CM, Baldock C
RgGuinier 4.7 nm
Dmax 20.5 nm
VolumePorod 102 nm3

SASDNT3 – Fibrillin-1 fragment PF3 crosslinked to latent transforming growth factor-beta-binding protein 1 C-terminus by transglutaminase 2

UniProt ID: Q14766-2 (1329-1721) Latent-transforming growth factor beta-binding protein 1

UniProt ID: P35555 (1-722) Fibrillin-1 PF3
Latent-transforming growth factor beta-binding protein 1Fibrillin-1 PF3 experimental SAS data
DAMMIF model
Sample: Latent-transforming growth factor beta-binding protein 1 monomer, 44 kDa Homo sapiens protein
Fibrillin-1 PF3 monomer, 78 kDa Homo sapiens protein
Buffer: 10 mM Hepes, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2017 Jul 20
Latent TGFβ complexes are transglutaminase cross-linked to fibrillin to facilitate TGFβ activation. Matrix Biol (2022)
Lockhart-Cairns MP, Cain SA, Dajani R, Steer R, Thomson J, Alanazi YF, Kielty CM, Baldock C
RgGuinier 7.4 nm
Dmax 29.6 nm
VolumePorod 759 nm3

SASDNU3 – Fibrillin PF2

UniProt ID: P35555 (330-722) Fibrillin-1
Fibrillin-1 experimental SAS data
DAMMIF model
Sample: Fibrillin-1 monomer, 44 kDa Homo sapiens protein
Buffer: Tris buffered saline, pH: 7.4
Experiment: SAXS data collected at ID02, ESRF on 2006 Feb 11
Transglutaminase-Mediated Cross-Linking of Tropoelastin to Fibrillin Stabilises the Elastin Precursor Prior to Elastic Fibre Assembly. J Mol Biol 432(21):5736-5751 (2020)
Lockhart-Cairns MP, Newandee H, Thomson J, Weiss AS, Baldock C, Tarakanova A
RgGuinier 4.3 nm
Dmax 15.0 nm
VolumePorod 84 nm3

SASDNV3 – Synthetic Human Elastin without domain 26A

UniProt ID: P15502-2 (27-724) Elastin
Elastin experimental SAS data
Elastin Kratky plot
Sample: Elastin monomer, 60 kDa Homo sapiens protein
Buffer: Phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at ID02, ESRF on 2011 Mar 15
Transglutaminase-Mediated Cross-Linking of Tropoelastin to Fibrillin Stabilises the Elastin Precursor Prior to Elastic Fibre Assembly. J Mol Biol 432(21):5736-5751 (2020)
Lockhart-Cairns MP, Newandee H, Thomson J, Weiss AS, Baldock C, Tarakanova A
RgGuinier 6.6 nm
Dmax 22.5 nm

SASDNW3 – Fibrillin-1 fragment PF2 crosslinked to tropoelastin by transglutaminase 2

UniProt ID: P35555 (330-722) Fibrillin-1

UniProt ID: P15502 (27-724) Elastin
Fibrillin-1Elastin experimental SAS data
DAMMIF model
Sample: Fibrillin-1 monomer, 44 kDa Homo sapiens protein
Elastin monomer, 60 kDa Homo sapiens protein
Buffer: Tris buffered saline, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Feb 21
Transglutaminase-Mediated Cross-Linking of Tropoelastin to Fibrillin Stabilises the Elastin Precursor Prior to Elastic Fibre Assembly. J Mol Biol 432(21):5736-5751 (2020)
Lockhart-Cairns MP, Newandee H, Thomson J, Weiss AS, Baldock C, Tarakanova A
RgGuinier 7.1 nm
Dmax 23.5 nm

SASDNX3 – Calcium-bound Calmodulin, including structural models

UniProt ID: P0DP23 (2-149) Calmodulin-1
Calmodulin-1 experimental SAS data
Calcium-bound Calmodulin, including structural models Rg histogram
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Nov 15
Dynamics and structural changes of calmodulin upon interaction with the antagonist calmidazolium. BMC Biol 20(1):176 (2022)
Léger C, Pitard I, Sadi M, Carvalho N, Brier S, Mechaly A, Raoux-Barbot D, Davi M, Hoos S, Weber P, Vachette P, Durand D, Haouz A, Guijarro JI, Ladant D, Chenal A
RgGuinier 2.2 nm
Dmax 7.2 nm
VolumePorod 33 nm3

SASDNY3 – Calcium-bound Calmodulin complexed with Calmidazolium

UniProt ID: P0DP23 (2-149) Calmodulin-1

UniProt ID: None (None-None) Calmidazolium
Calmodulin-1Calmidazolium experimental SAS data
Sample: Calmodulin-1 monomer, 17 kDa Homo sapiens protein
Calmidazolium monomer, 1 kDa
Buffer: 20 mM Hepes, 150 mM NaCl, 2 mM CaCl2, pH: 7.4
Experiment: SAXS data collected at SWING, SOLEIL on 2020 Nov 15
Dynamics and structural changes of calmodulin upon interaction with the antagonist calmidazolium. BMC Biol 20(1):176 (2022)
Léger C, Pitard I, Sadi M, Carvalho N, Brier S, Mechaly A, Raoux-Barbot D, Davi M, Hoos S, Weber P, Vachette P, Durand D, Haouz A, Guijarro JI, Ladant D, Chenal A
RgGuinier 1.7 nm
Dmax 5.2 nm
VolumePorod 30 nm3

SASDNZ3 – Heterodimerization between the nuclear receptor subfamily proteins PXR and CAR

UniProt ID: O75469 (130-434) Nuclear receptor subfamily 1 group I member 2

UniProt ID: Q14994 (103-352) Nuclear receptor subfamily 1 group I member 3
Nuclear receptor subfamily 1 group I member 2Nuclear receptor subfamily 1 group I member 3 experimental SAS data
DAMMIF model
Sample: Nuclear receptor subfamily 1 group I member 2 monomer, 39 kDa Homo sapiens protein
Nuclear receptor subfamily 1 group I member 3 monomer, 32 kDa Homo sapiens protein
Buffer: 25 mM Hepes, 150 mM NaCl, 5% glycerol, 5 mM DTT, pH: 7.9
Experiment: SAXS data collected at 16-ID (LiX), National Synchrotron Light Source II (NSLS-II) on 2021 Oct 8
Molecular basis of crosstalk in nuclear receptors: heterodimerization between PXR and CAR and the implication in gene regulation
Shirish chodankar
RgGuinier 2.7 nm
Dmax 10.1 nm
VolumePorod 56 nm3

SASDLF9 – 200-310 region of Hendra virus P/V/W protein (PNT3)

UniProt ID: P0C1C6 (200-310) Protein W
Protein W experimental SAS data
200-310 region of Hendra virus P/V/W protein (PNT3) Rg histogram
Sample: Protein W monomer, 15 kDa Hendra virus (isolate … protein
Buffer: 50 mM sodium phosphate, 5 mM EDTA, pH: 6.5
Experiment: SAXS data collected at SWING, SOLEIL on 2021 Jun 12
Identification of a Region in the Common Amino-terminal Domain of Hendra Virus P, V, and W Proteins Responsible for Phase Transition and Amyloid Formation Biomolecules 11(9):1324 (2021)
Salladini E, Gondelaud F, Nilsson J, Pesce G, Bignon C, Murrali M, Fabre R, Pierattelli R, Kajava A, Horvat B, Gerlier D, Mathieu C, Longhi S
RgGuinier 3.4 nm
Dmax 15.5 nm
VolumePorod 38 nm3