SASDCR6 – Rap guanine nucleotide exchange factor 3 (isoform3) - binary form with cAMP

Rap guanine nucleotide exchange factor 3 (dimer) experimental SAS data
CORAL model
Sample: Rap guanine nucleotide exchange factor 3 (dimer) dimer, 200 kDa Homo sapiens protein
Buffer: 1mM EDTA, 10mM DTT, 500mM NaCl, 1mM cAMP, and 10mM Tris, pH: 9
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2012 Jan 30
Conformational States of Exchange Protein Directly Activated by cAMP (EPAC1) Revealed by Ensemble Modeling and Integrative Structural Biology. Cells 9(1) (2019)
White MA, Tsalkova T, Mei FC, Cheng X
RgGuinier 5.3 nm
Dmax 15.7 nm
VolumePorod 415 nm3

SASDCS6 – Rap guanine nucleotide exchange factor 3 (isoform3) bound to RAS related protein 1b - with cAMP

Rap guanine nucleotide exchange factor 3RAS related protein 1b experimental SAS data
SWISSMODEL model
Sample: Rap guanine nucleotide exchange factor 3 monomer, 100 kDa Homo sapiens protein
RAS related protein 1b monomer, 18 kDa Mus musculus protein
Buffer: 1mM EDTA, 10mM DTT, 500mM NaCl, 1mM cAMP, and 10mM Tris, pH: 9
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2013 Apr 1
Conformational States of Exchange Protein Directly Activated by cAMP (EPAC1) Revealed by Ensemble Modeling and Integrative Structural Biology. Cells 9(1) (2019)
White MA, Tsalkova T, Mei FC, Cheng X
RgGuinier 4.1 nm
Dmax 14.2 nm
VolumePorod 207 nm3

SASDF45 – Leukocidin/Integrin alpha-M complex (LukGH-huCD11b-I) in the presence of a neutralizing antibody Fab fragment

Leukocidin GLeukocidin HLukGH neutralizing antibodyIntegrin alpha-M experimental SAS data
PYMOL model
Sample: Leukocidin G monomer, 36 kDa Staphylococcus aureus protein
Leukocidin H monomer, 38 kDa Staphylococcus aureus protein
LukGH neutralizing antibody monomer, 47 kDa Homo sapiens protein
Integrin alpha-M monomer, 22 kDa Homo sapiens protein
Buffer: 20 mM Hepes, 300 mM NaCl, 1 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 17
Molecular mechanism of leukocidin GH-integrin CD11b/CD18 recognition and species specificity. Proc Natl Acad Sci U S A (2019)
Trstenjak N, Milić D, Graewert MA, Rouha H, Svergun D, Djinović-Carugo K, Nagy E, Badarau A
RgGuinier 5.0 nm
Dmax 18.0 nm
VolumePorod 178 nm3

SASDF55 – Leukocidin (LukGH) from Staphylococcus aureus in complex with a neutralizing antibody

Leukocidin GLeukocidin HLukGH neutralizing antibody experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Leukocidin G monomer, 36 kDa Staphylococcus aureus protein
Leukocidin H monomer, 38 kDa Staphylococcus aureus protein
LukGH neutralizing antibody monomer, 47 kDa Homo sapiens protein
Buffer: 20 mM Hepes, 300 mM NaCl, 1 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 17
Molecular mechanism of leukocidin GH-integrin CD11b/CD18 recognition and species specificity. Proc Natl Acad Sci U S A (2019)
Trstenjak N, Milić D, Graewert MA, Rouha H, Svergun D, Djinović-Carugo K, Nagy E, Badarau A
RgGuinier 4.7 nm
Dmax 16.0 nm
VolumePorod 152 nm3

SASDGV5 – The nucleotide binding domain of Lipid A export ATP-binding/permease protein MsbA - data from stop-and-flow time-resolved SAXS (12 s time course)

Lipid A export ATP-binding/permease protein MsbA - Nucleotide binding domain experimental SAS data
Lipid A export ATP-binding/permease protein MsbA - Nucleotide binding domain Kratky plot
Sample: Lipid A export ATP-binding/permease protein MsbA - Nucleotide binding domain monomer, 27 kDa Escherichia coli protein
Buffer: 20 mM Tris, 150 mM NaCl, 5 mM MgCl2, 0.45 mM Mg2+-ATP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Dec 8
Structural Kinetics of MsbA Investigated by Stopped-Flow Time-Resolved Small-Angle X-Ray Scattering. Structure (2019)
Josts I, Gao Y, Monteiro DCF, Niebling S, Nitsche J, Veith K, Gräwert TW, Blanchet CE, Schroer MA, Huse N, Pearson AR, Svergun DI, Tidow H
RgGuinier 2.1 nm
Dmax 6.8 nm
VolumePorod 50 nm3

SASDES7 – Stator protein complex FlaG/FlaF

Conserved flagellar protein FStator protein FlaG soluble domain experimental SAS data
MULTIFOXS model
Sample: Conserved flagellar protein F dimer, 32 kDa Sulfolobus acidocaldarius protein
Stator protein FlaG soluble domain dimer, 30 kDa Sulfolobus acidocaldarius protein
Buffer: 25 mM citric acid/sodium citrate, 150mM NaCl, 3% Glycerol, pH: 3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Nov 10
The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility. Nat Microbiol (2019)
Tsai CL, Tripp P, Sivabalasarma S, Zhang C, Rodriguez-Franco M, Wipfler RL, Chaudhury P, Banerjee A, Beeby M, Whitaker RJ, Tainer JA, Albers SV
RgGuinier 3.2 nm
Dmax 12.5 nm
VolumePorod 109 nm3

SASDET7 – Stator protein complex FlaG-V118K/FlaF

Conserved flagellar protein FStator protein FlaG-V118K soluble domain experimental SAS data
MULTIFOXS model
Sample: Conserved flagellar protein F dimer, 32 kDa Sulfolobus acidocaldarius protein
Stator protein FlaG-V118K soluble domain dimer, 30 kDa Sulfolobus acidocaldarius protein
Buffer: 25 mM citric acid/sodium citrate, 150mM NaCl, 3% Glycerol, pH: 3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Nov 10
The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility. Nat Microbiol (2019)
Tsai CL, Tripp P, Sivabalasarma S, Zhang C, Rodriguez-Franco M, Wipfler RL, Chaudhury P, Banerjee A, Beeby M, Whitaker RJ, Tainer JA, Albers SV
RgGuinier 3.2 nm
Dmax 12.5 nm
VolumePorod 108 nm3

SASDEU7 – Stator protein FlaG soluble domain

Conserved flagellar protein FlaG soluble domain experimental SAS data
Conserved flagellar protein FlaG soluble domain Kratky plot
Sample: Conserved flagellar protein FlaG soluble domain monomer, 15 kDa Sulfolobus acidocaldarius protein
Buffer: 25 mM citric acid/sodium citrate, 150mM NaCl, 3% Glycerol, pH: 3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Nov 10
The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility. Nat Microbiol (2019)
Tsai CL, Tripp P, Sivabalasarma S, Zhang C, Rodriguez-Franco M, Wipfler RL, Chaudhury P, Banerjee A, Beeby M, Whitaker RJ, Tainer JA, Albers SV
RgGuinier 3.7 nm
Dmax 18.0 nm
VolumePorod 133 nm3

SASDEV7 – Stator protein complex FlaG/FlaF-I96Y

Stator protein FlaG soluble domainConserved flagellar protein FlaF-I96Y soluble domain experimental SAS data
BILBOMD model
Sample: Stator protein FlaG soluble domain dimer, 30 kDa Sulfolobus acidocaldarius protein
Conserved flagellar protein FlaF-I96Y soluble domain dimer, 33 kDa Sulfolobus acidocaldarius protein
Buffer: 25 mM citric acid/sodium citrate, 150mM NaCl, 3% Glycerol, pH: 3
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Nov 10
The structure of the periplasmic FlaG-FlaF complex and its essential role for archaellar swimming motility. Nat Microbiol (2019)
Tsai CL, Tripp P, Sivabalasarma S, Zhang C, Rodriguez-Franco M, Wipfler RL, Chaudhury P, Banerjee A, Beeby M, Whitaker RJ, Tainer JA, Albers SV
RgGuinier 2.7 nm
Dmax 8.2 nm
VolumePorod 90 nm3

SASDEN8 – Intracellular region of the human Cyclin and CBS domain divalent metal cation transport mediator-4 in complex with Phosphatase of Regenerating Liver-1 and MgATP

CNNM4_BAT-cNMP-CtailProtein tyrosine phosphatase type IVA 1 experimental SAS data
CORAL model
Sample: CNNM4_BAT-cNMP-Ctail dimer, 96 kDa Homo sapiens protein
Protein tyrosine phosphatase type IVA 1 dimer, 40 kDa Mus musculus protein
Buffer: HEPES buffer pH 7.4, 200 mM NaCl , 1mM DTT, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 Sep 17
Structural Insights into the Intracellular Region of the Human Magnesium Transport Mediator CNNM4. Int J Mol Sci 20(24) (2019)
Giménez-Mascarell P, Oyenarte I, González-Recio I, Fernández-Rodríguez C, Corral-Rodríguez MÁ, Campos-Zarraga I, Simón J, Kostantin E, Hardy S, Díaz Quintana A, Zubillaga Lizeaga M, Merino N, Diercks ...
RgGuinier 4.4 nm
Dmax 18.3 nm
VolumePorod 216 nm3

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