Browse by MODEL: Hybrid

SASDHR9 – GntR-type transcriptional regulator NanR from Escherichia coli

HTH-type transcriptional repressor NanR experimental SAS data
CUSTOM IN-HOUSE model
Sample: HTH-type transcriptional repressor NanR dimer, 59 kDa Escherichia coli protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.1 % (w/v) sodium azide, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Apr 20
Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism (2020)
Horne C, Venugopal H, Panjikar S, Henrickson A, Brookes E, North R, Murphy J, Friemann R, Griffin M, Ramm G, Demeler B, Dobson R
RgGuinier 3.2 nm
Dmax 10.5 nm
VolumePorod 110 nm3

SASDHS9 – GntR-type transcriptional regulator NanR from Escherichia coli in the presence of N-acetylneuraminic acid

HTH-type transcriptional repressor NanR experimental SAS data
CUSTOM IN-HOUSE model
Sample: HTH-type transcriptional repressor NanR dimer, 59 kDa Escherichia coli protein
Buffer: 20 mM Tris, 150 mM NaCl, 20 mM Neu5Ac and 0.1 % (w/v) sodium azide, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Apr 20
Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism (2020)
Horne C, Venugopal H, Panjikar S, Henrickson A, Brookes E, North R, Murphy J, Friemann R, Griffin M, Ramm G, Demeler B, Dobson R
RgGuinier 3.1 nm
Dmax 10.1 nm
VolumePorod 105 nm3

SASDHT9 – Dimeric NanR-DNA hetero-complex from Escherichia coli

HTH-type transcriptional repressor NanR(GGTATA)2 repeat DNA experimental SAS data
CUSTOM IN-HOUSE model
Sample: HTH-type transcriptional repressor NanR dimer, 59 kDa Escherichia coli protein
(GGTATA)2 repeat DNA monomer, 11 kDa DNA
Buffer: 20 mM Tris, 150 mM NaCl, 0.1 % (w/v) sodium azide, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Apr 20
Mechanism of NanR gene repression and allosteric induction of bacterial sialic acid metabolism (2020)
Horne C, Venugopal H, Panjikar S, Henrickson A, Brookes E, North R, Murphy J, Friemann R, Griffin M, Ramm G, Demeler B, Dobson R
RgGuinier 3.3 nm
Dmax 9.8 nm
VolumePorod 108 nm3

SASDFV6 – DNA-binding protein HU-alpha, E38K/V42L double mutant

DNA-binding protein HU-alpha, E38K/V42L double mutant experimental SAS data
CHIMERA model
Sample: DNA-binding protein HU-alpha, E38K/V42L double mutant decamer, 95 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 1 mM PMSF, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Apr 23
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling (supplementary)
Soumya G Remesh
RgGuinier 3.0 nm
Dmax 10.5 nm
VolumePorod 53 nm3

SASDFW6 – DNA-binding protein HU-alpha, E38K/V42L double mutant bound to 80 bp DNA (ratio DNA:Protein 1:2)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E38K/V42L double mutant experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E38K/V42L double mutant tetramer, 38 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 1 mM PMSF, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Apr 23
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling (supplementary)
Soumya G Remesh
RgGuinier 5.7 nm
Dmax 31.3 nm
VolumePorod 297 nm3

SASDFX6 – DNA-binding protein HU-alpha, E38K/V42L double mutant bound to 80 bp DNA (ratio DNA:Protein 1:4)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E38K/V42L double mutant experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E38K/V42L double mutant tetramer, 38 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 1 mM PMSF, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Apr 23
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling (supplementary)
Soumya G Remesh
RgGuinier 5.7 nm
Dmax 25.7 nm
VolumePorod 195 nm3

SASDFY6 – DNA-binding protein HU-alpha, E38K/V42L double mutant bound to 80 bp DNA (ratio DNA:Protein 1:8)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E38K/V42L double mutant experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E38K/V42L double mutant octamer, 76 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 1 mM PMSF, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Apr 23
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling (supplementary)
Soumya G Remesh
RgGuinier 5.8 nm
Dmax 28.1 nm
VolumePorod 296 nm3

SASDFZ6 – DNA-binding protein HU-alpha, E38K/V42L double mutant bound to 80 bp DNA (ratio DNA:Protein 1:16)

80bp_DNA Forward80bp_DNA ReverseDNA-binding protein HU-alpha, E38K/V42L double mutant experimental SAS data
CHIMERA model
Sample: 80bp_DNA Forward monomer, 25 kDa Escherichia coli DNA
80bp_DNA Reverse monomer, 25 kDa Escherichia coli DNA
DNA-binding protein HU-alpha, E38K/V42L double mutant 16-mer, 153 kDa Linked to wild-type … protein
Buffer: 50 mM Tris-HCl, 150 mM NaCl, 1 mM DTT, 1 mM PMSF, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2015 Apr 23
Nucleoid remodeling during environmental adaptation is regulated by HU-dependent DNA bundling (supplementary)
Soumya G Remesh
RgGuinier 6.3 nm
Dmax 27.3 nm
VolumePorod 401 nm3

SASDHQ5 – Ile-Leu-Gln-Ile-Asn-Ser (ILQINS) hexapeptide self-assembly

Ile-Leu-Gln-Ile-Asn-Ser peptide experimental SAS data
OTHER model
Sample: Ile-Leu-Gln-Ile-Asn-Ser peptide, 1 kDa synthetic construct protein
Buffer: pure (MQ, 18 MΩ) Water, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2018 Nov 1
Amyloid Evolution: Antiparallel Replaced by Parallel. Biophys J (2020)
Zanjani AAH, Reynolds NP, Zhang A, Schilling T, Mezzenga R, Berryman JT

SASDD88 – The BRCT domain from Mycobacterium tuberculosis DNA ligase

M.tb. LigA BRCT domain (DNA ligase A) experimental SAS data
DAMMIN model
Sample: M.tb. LigA BRCT domain (DNA ligase A) monomer, 13 kDa Mycobacterium tuberculosis protein
Buffer: 50 mM Tris-HCl 500 mM NaCl 5mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2018 Jun 2
M. tuberculosis class II apurinic/ apyrimidinic-endonuclease/3'-5' exonuclease (XthA) engages with NAD+-dependent DNA ligase A (LigA) to counter futile cleavage and ligation cycles in base excision repair. Nucleic Acids Res (2020)
Khanam T, Afsar M, Shukla A, Alam F, Kumar S, Soyar H, Dolma K, Pasupuleti M, Srivastava KK, Ampapathi RS, Ramachandran R
RgGuinier 1.6 nm
Dmax 3.7 nm
VolumePorod 23 nm3