Browse by MACROMOLECULE type: protein

SASDGS5 – MvaT (low salt data set)

MvaT(mutant) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: MvaT(mutant) dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 20 mM Bis-Tris 50 mM KCl, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2018 May 11
Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins. Nucleic Acids Res (2020)
Qin L, Bdira FB, Sterckx YGJ, Volkov AN, Vreede J, Giachin G, van Schaik P, Ubbink M, Dame RT
RgGuinier 3.6 nm
Dmax 14.7 nm
VolumePorod 47 nm3

SASDGT5 – MvaT (high salt data set)

MvaT(mutant) experimental SAS data
OTHER [STATIC IMAGE] model
Sample: MvaT(mutant) dimer, 28 kDa Pseudomonas aeruginosa protein
Buffer: 20 mM Bis-Tris 300 mM KCl, pH: 6
Experiment: SAXS data collected at BM29, ESRF on 2018 May 11
Structural basis for osmotic regulation of the DNA binding properties of H-NS proteins. Nucleic Acids Res (2020)
Qin L, Bdira FB, Sterckx YGJ, Volkov AN, Vreede J, Giachin G, van Schaik P, Ubbink M, Dame RT
RgGuinier 3.8 nm
Dmax 15.8 nm
VolumePorod 50 nm3

SASDG95 – Phosphorylated resistance to inhibitors of cholinesterase 8 homolog A (Ric-8A, 1-491) and G protein complex

Resistance to inhibitors of cholinesterase 8 homolog AGuanine nucleotide-binding protein G(i) subunit alpha-1 experimental SAS data
DAMMIF model
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 56 kDa Rattus norvegicus protein
Guanine nucleotide-binding protein G(i) subunit alpha-1 monomer, 38 kDa Rattus norvegicus protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Jul 30
Structure of the G protein chaperone and guanine nucleotide exchange factor Ric-8A bound to Gαi1 Nature Communications 11(1) (2020)
McClelland L, Zhang K, Mou T, Johnston J, Yates-Hansen C, Li S, Thomas C, Doukov T, Triest S, Wohlkonig A, Tall G, Steyaert J, Chiu W, Sprang S
RgGuinier 3.5 nm
Dmax 11.5 nm
VolumePorod 120 nm3

SASDHP7 – Haloalkane dehalogenase variant DhaA115 - monomeric fraction

Haloalkane dehalogenase variant DhaA115 -monomeric fraction experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Haloalkane dehalogenase variant DhaA115 -monomeric fraction monomer, 34 kDa Rhodococcus rhodochrous protein
Buffer: 50 mM potassium phosphate buffer (41 mM K₂HPO₄, 9mM KH₂PO₄), pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2019 Aug 22
Decoding the intricate network of molecular interactions of a hyperstable engineered biocatalyst Chemical Science 11(41):11162-11178 (2020)
Markova K, Chmelova K, Marques S, Carpentier P, Bednar D, Damborsky J, Marek M
RgGuinier 1.9 nm
Dmax 6.0 nm
VolumePorod 41 nm3

SASDHQ7 – Haloalkane dehalogenase variant DhaA115 - dimeric fraction

Haloalkane dehalogenase variant DhaA115 - dimeric fraction experimental SAS data
CORAL model
Sample: Haloalkane dehalogenase variant DhaA115 - dimeric fraction dimer, 69 kDa Rhodococcus rhodochrous protein
Buffer: 50 mM potassium phosphate buffer (41 mM K₂HPO₄, 9mM KH₂PO₄), pH: 7.5
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2019 Aug 22
Decoding the intricate network of molecular interactions of a hyperstable engineered biocatalyst Chemical Science 11(41):11162-11178 (2020)
Markova K, Chmelova K, Marques S, Carpentier P, Bednar D, Damborsky J, Marek M
RgGuinier 2.9 nm
Dmax 8.9 nm
VolumePorod 78 nm3

SASDKE4 – Polymorphic DNA protection during starvation protein (Dps)-DNA сo-сrystals

DNA protection during starvation protein experimental SAS data
DNA protection during starvation protein Kratky plot
Sample: DNA protection during starvation protein dodecamer, 224 kDa Escherichia coli (strain … protein
Buffer: 10 mM Tris-HCl, 100 mM NaCl, 0.5 mM EDTA, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Oct 28
Polymorphic Protective Dps-DNA Co-Crystals by Cryo Electron Tomography and Small Angle X-Ray Scattering. Biomolecules 10(1) (2019)
Kamyshinsky R, Chesnokov Y, Dadinova L, Mozhaev A, Orlov I, Petoukhov M, Orekhov A, Shtykova E, Vasiliev A

SASDEN3 – Perivitellin PmPV2

P. maculata perivitellin 2 experimental SAS data
DAMMIN model
Sample: P. maculata perivitellin 2 dimer, 188 kDa Pomacea maculata protein
Buffer: 20 mM Tris, pH: 7
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2015 Mar 26
Exaptation of two ancient immune proteins into a new dimeric pore-forming toxin in snails. J Struct Biol 211(2):107531 (2020)
Giglio ML, Ituarte S, Milesi V, Dreon MS, Brola TR, Caramelo J, Ip JCH, Maté S, Qiu JW, Otero LH, Heras H
RgGuinier 4.4 nm
Dmax 14.3 nm
VolumePorod 267 nm3

SASDCQ6 – Rap guanine nucleotide exchange factor 3 (isoform3) - apo form

Rap guanine nucleotide exchange factor 3 experimental SAS data
SWISSMODEL model
Sample: Rap guanine nucleotide exchange factor 3 monomer, 100 kDa Homo sapiens protein
Buffer: 1mM EDTA, 10mM DTT, 500mM NaCl, and 10mM Tris, pH: 9
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2012 Sep 7
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 3.4 nm
Dmax 11.0 nm
VolumePorod 180 nm3

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