SASBDB entries for UniProt ID:

SASDLW6 – High mannose glycan contactin 1 ectodomain, 11.1 μM

UniProt ID: P12960 (21-996) Contactin-1 I433V

Contactin-1 I433V experimental SAS data
Contactin-1 I433V Kratky plot
Sample: Contactin-1 I433V dimer, 220 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Structural insights into the contactin 1 – neurofascin 155 adhesion complex Nature Communications 13(1) (2022)
Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B
RgGuinier 6.8 nm
Dmax 27.0 nm
VolumePorod 275 nm3

SASDLX6 – High mannose glycan contactin 1 ectodomain, 5.5 μM

UniProt ID: P12960 (21-996) Contactin-1 I433V

Contactin-1 I433V experimental SAS data
Contactin-1 I433V Kratky plot
Sample: Contactin-1 I433V dimer, 220 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Structural insights into the contactin 1 – neurofascin 155 adhesion complex Nature Communications 13(1) (2022)
Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B
RgGuinier 6.8 nm
Dmax 27.0 nm
VolumePorod 270 nm3

SASDLY6 – High mannose glycan contactin 1 ectodomain, 2.4 μM

UniProt ID: P12960 (21-996) Contactin-1 I433V

Contactin-1 I433V experimental SAS data
CUSTOM IN-HOUSE model
Sample: Contactin-1 I433V dimer, 220 kDa Mus musculus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 16
Structural insights into the contactin 1 – neurofascin 155 adhesion complex Nature Communications 13(1) (2022)
Chataigner L, Gogou C, den Boer M, Frias C, Thies-Weesie D, Granneman J, Heck A, Meijer D, Janssen B
RgGuinier 6.8 nm
Dmax 19.5 nm
VolumePorod 254 nm3

SASDLZ6 – Hexamer - monomer equilibrium of Glutamate Synthase

UniProt ID: Q05755 (1-1508) Glutamate synthase [NADPH] large chain

UniProt ID: Q05756 (27-482) Glutamate synthase [NADPH] small chain

Glutamate synthase [NADPH] large chainGlutamate synthase [NADPH] small chain experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Glutamate synthase [NADPH] large chain hexamer, 968 kDa Azospirillum brasilense protein
Glutamate synthase [NADPH] small chain hexamer, 296 kDa Azospirillum brasilense protein
Buffer: 25 mM Hepes/KOH, 1 mM EDTA, 1 mM dithiothreitol, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Feb 19
The Subnanometer Resolution Structure of the Glutamate Synthase 1.2-MDa Hexamer by Cryoelectron Microscopy and Its Oligomerization Behavior in Solution Journal of Biological Chemistry 283(13):8237-8249 (2008)
Cottevieille M, Larquet E, Jonic S, Petoukhov M, Caprini G, Paravisi S, Svergun D, Vanoni M, Boisset N
RgGuinier 7.7 nm
Dmax 22.4 nm

SASDL27 – N-Oct-3 POU transcription factor domain in complex with rat CRH DNA

UniProt ID: P20265 (254-420) POU domain, class 3, transcription factor 2

UniProt ID: None (None-None) Rat CRH DNA

POU domain, class 3, transcription factor 2Rat CRH DNA experimental SAS data
CUSTOM IN-HOUSE model
Sample: POU domain, class 3, transcription factor 2 monomer, 19 kDa Homo sapiens protein
Rat CRH DNA monomer, 15 kDa Rattus norvegicus DNA
Buffer: 50 mM Tris, 0.4 M NaCl, 2% glycerol, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2003 Oct 9
Fine-tuning of intrinsic N-Oct-3 POU domain allostery by regulatory DNA targets Nucleic Acids Research 35(13):4420-4432 (2007)
Alazard R, Mourey L, Ebel C, Konarev P, Petoukhov M, Svergun D, Erard M
RgGuinier 2.9 nm
Dmax 11.0 nm
VolumePorod 41 nm3

SASDL37 – N-Oct-3 POU transcription factor domain in complex with human DR-alpha DNA

UniProt ID: P20265 (254-420) POU domain, class 3, transcription factor 2

UniProt ID: None (None-None) Human DR-alpha DNA

POU domain, class 3, transcription factor 2Human DR-alpha DNA experimental SAS data
CUSTOM IN-HOUSE model
Sample: POU domain, class 3, transcription factor 2 monomer, 19 kDa Homo sapiens protein
Human DR-alpha DNA monomer, 15 kDa Homo sapiens DNA
Buffer: 50 mM Tris, 0.4 M NaCl, 2% glycerol, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2004 May 26
Fine-tuning of intrinsic N-Oct-3 POU domain allostery by regulatory DNA targets Nucleic Acids Research 35(13):4420-4432 (2007)
Alazard R, Mourey L, Ebel C, Konarev P, Petoukhov M, Svergun D, Erard M
RgGuinier 2.9 nm
Dmax 11.0 nm
VolumePorod 44 nm3

SASDL47 – Oligomeric composition of AXH Domain of Ataxin-1 (wild type and A567G, I580A mutants)

UniProt ID: P54253 (567-689) Ataxin-1

Ataxin-1 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Ataxin-1 monomer, 14 kDa Homo sapiens protein
Buffer: 20 mM Tris-HCl, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 21
Self-assembly and conformational heterogeneity of the AXH domain of ataxin-1: an unusual example of a chameleon fold. Biophys J 104(6):1304-13 (2013)
de Chiara C, Rees M, Menon RP, Pauwels K, Lawrence C, Konarev PV, Svergun DI, Martin SR, Chen YW, Pastore A
RgGuinier 5.5 nm

SASDL57 – Thermus thermophilus 3-isopropylmalate dehydrogenase

UniProt ID: P61495 (1-345) 3-isopropylmalate dehydrogenase

3-isopropylmalate dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: 3-isopropylmalate dehydrogenase dimer, 73 kDa Thermus thermophilus protein
Buffer: 25 mM MOPS/NaOH, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 3
Glutamate 270 plays an essential role in K(+)-activation and domain closure of Thermus thermophilus isopropylmalate dehydrogenase. FEBS Lett 589(2):240-5 (2015)
Gráczer É, Palló A, Oláh J, Szimler T, Konarev PV, Svergun DI, Merli A, Závodszky P, Weiss MS, Vas M
RgGuinier 2.8 nm

SASDL67 – Mutation of the Active Site Residues of Thermus thermophilus 3‑Isopropylmalate Dehydrogenase

UniProt ID: P61495 (1-345) 3-isopropylmalate dehydrogenase

3-isopropylmalate dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: 3-isopropylmalate dehydrogenase dimer, 73 kDa Thermus thermophilus protein
Buffer: 25 mM MOPS/NaOH, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2012 Nov 16
Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure. Biochemistry 55(3):560-74 (2016)
Gráczer É, Szimler T, Garamszegi A, Konarev PV, Lábas A, Oláh J, Palló A, Svergun DI, Merli A, Závodszky P, Weiss MS, Vas M
RgGuinier 2.8 nm

SASDL97 – Ru-MtrCAB complex formed by reconstitution of Ru-MtrC and MtrAB

UniProt ID: Q8EG35 (35-333) Extracelllular iron oxide respiratory system periplasmic decaheme cytochrome c component MtrA

UniProt ID: Q8EG34 (26-671) Extracellular iron oxide respiratory system surface decaheme cytochrome c component MtrC

UniProt ID: Q8CVD4 (22-697) Extracellular iron oxide respiratory system outer membrane component MtrB

Extracelllular iron oxide respiratory system periplasmic decaheme cytochrome c component MtrAExtracellular iron oxide respiratory system surface decaheme cytochrome c component MtrCExtracellular iron oxide respiratory system outer membrane component MtrB experimental SAS data
DAMMIN model
Sample: Extracelllular iron oxide respiratory system periplasmic decaheme cytochrome c component MtrA monomer, 39 kDa Shewanella oneidensis (strain … protein
Extracellular iron oxide respiratory system surface decaheme cytochrome c component MtrC monomer, 77 kDa Shewanella oneidensis (strain … protein
Extracellular iron oxide respiratory system outer membrane component MtrB monomer, 75 kDa Shewanella oneidensis (strain … protein
Buffer: 20 mM HEPES, 100 mM NaCl, 2.8 mM Fos-choline 12, 13% D2O, pH: 7.8
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2020 Jan 13
Bespoke Biomolecular Wires for Transmembrane Electron Transfer: Spontaneous Assembly of a Functionalized Multiheme Electron Conduit Frontiers in Microbiology 12 (2021)
Piper S, Edwards M, van Wonderen J, Casadevall C, Martel A, Jeuken L, Reisner E, Clarke T, Butt J
RgGuinier 4.7 nm
Dmax 16.6 nm
VolumePorod 154 nm3