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49 hits found for Peptide

SASDFE2 – ...Peptide (LAP)

Latency Associated Peptide experimental SAS data
Latency Associated Peptide Kratky plot
Sample: ...Peptide dimer, 58 kDa Homo sapiens protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Oct 4
Structural consequences of transforming growth factor beta-1 activation from near-therapeutic X-ray doses. J Synchrotron Radiat 26(Pt 4):967-979 (2019)
Stachowski T, Grant TD, Snell EH
RgGuinier 4.1 nm
Dmax 17.5 nm
VolumePorod 179 nm3

SASDHZ2 – 14-3-3 protein beta isoform

14-3-3 protein beta/alpha experimental SAS data
BUNCH model
Sample: 14-3-3 protein beta/alpha dimer, 58 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
...peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 92 nm3

SASDH33 – Rho GTPase-activating protein 22

Rho GTPase-activating protein 22 experimental SAS data
BUNCH model
Sample: Rho GTPase-activating protein 22 monomer, 47 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
...peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.2 nm
Dmax 12.0 nm
VolumePorod 88 nm3

SASDD53 – ...peptide repeat domain of Bacterial cellulose synthesis subunit C

Bacterial cellulose synthesis subunit C experimental SAS data
DAMMIF model
Sample: Bacterial cellulose synthesis subunit C monomer, 71 kDa Enterobacter sp. CJF-002 protein
Buffer: 50 mM HEPES, 100 mM KCl, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2017 Apr 24
Crystal structure of the flexible tandem repeat domain of bacterial cellulose synthesis subunit C. Sci Rep 7(1):13018 (2017)
Nojima S, Fujishima A, Kato K, Ohuchi K, Shimizu N, Yonezawa K, Tajima K, Yao M
RgGuinier 5.1 nm
Dmax 18.5 nm
VolumePorod 115 nm3

SASDC63 – ...peptide (FPV039:BAK)

Bcl-2-like protein FPV039Uncharacterized protein (BAK1) experimental SAS data
Bcl-2-like protein FPV039 Uncharacterized protein (BAK1) Kratky plot
Sample: Bcl-2-like protein FPV039 monomer, 17 kDa Fowlpox virus protein
Uncharacterized protein (BAK1) monomer, 3 kDa Gallus gallus protein
Buffer: 20 mM trisodium citrate pH, 200 mM NaCl, pH: 6
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Oct 2
Structural basis of apoptosis inhibition by the fowlpox virus protein FPV039. J Biol Chem 292(22):9010-9021 (2017)
Anasir MI, Caria S, Skinner MA, Kvansakul M
RgGuinier 2.0 nm

SASDH83 – Chemically crossed linked complex between Rho GTPase-activating protein 22 (ARHGAP22) and the beta isoform of the 14-3-3 protein beta/alpha

14-3-3 protein beta/alphaRho GTPase-activating protein 22 experimental SAS data
CORAL model
Sample: 14-3-3 protein beta/alpha dimer, 58 kDa Homo sapiens protein
Rho GTPase-activating protein 22 monomer, 47 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2 mM 2-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2011 Apr 7
...peptide binding mode. PLoS One 7(8):e41731 (2012)
Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 195 nm3

SASDC44 – Envelope of Col H PKD-CBD complexed with mini-collagen

ColH proteinCollagenous Peptide model [(PPG)10] experimental SAS data
DAMMIF model
Sample: ColH protein monomer, 24 kDa Hathewaya histolytica protein
...Peptide model [(PPG)10] trimer, 9 kDa synthetic construct protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Oct 12
Ca2+ -induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation. FEBS J 285(17):3254-3269 (2018)
Caviness P, Bauer R, Tanaka K, Janowska K, Roeser JR, Harter D, Sanders J, Ruth C, Matsushita O, Sakon J
RgGuinier 2.7 nm
Dmax 12.0 nm
VolumePorod 28 nm3

SASDC54 – Envelope of Col H PKD-PKD-CBD complexed with mini-collagen

ColH proteinCollagenous Peptide model [(PPG)10] experimental SAS data
DAMMIF model
Sample: ColH protein monomer, 34 kDa Hathewaya histolytica protein
...Peptide model [(PPG)10] trimer, 10 kDa synthetic construct protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Oct 12
Ca2+ -induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation. FEBS J 285(17):3254-3269 (2018)
Caviness P, Bauer R, Tanaka K, Janowska K, Roeser JR, Harter D, Sanders J, Ruth C, Matsushita O, Sakon J
RgGuinier 3.3 nm
Dmax 14.2 nm
VolumePorod 38 nm3

SASDC64 – Envelope of Col G PKD-CBD-CBD complexed with mini-collagen

Collagenous Peptide model [(PPG)10]ColG Collagenase experimental SAS data
DAMMIF model
Sample: ...Peptide model [(PPG)10] trimer, 9 kDa synthetic construct protein
ColG Collagenase monomer, 37 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Oct 12
Ca2+ -induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation. FEBS J 285(17):3254-3269 (2018)
Caviness P, Bauer R, Tanaka K, Janowska K, Roeser JR, Harter D, Sanders J, Ruth C, Matsushita O, Sakon J
RgGuinier 4.1 nm
Dmax 19.3 nm
VolumePorod 70 nm3

SASDAN4 – ...peptide complex

CalmodulinC-terminal region of human myelin basic protein experimental SAS data
SASREF model
Sample: Calmodulin monomer, 17 kDa Homo sapiens protein
C-terminal region of human myelin basic protein monomer, 2 kDa Homo sapiens protein
Buffer: 25 mM Tris75 200 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III on 2006 Nov 28
Interaction between the C-terminal region of human myelin basic protein and calmodulin: analysis of complex formation and solution structure. BMC Struct Biol 8:10 (2008)
Majava V, Petoukhov MV, Hayashi N, Pirilä P, Svergun DI, Kursula P
RgGuinier 2.1 nm
Dmax 7.0 nm
VolumePorod 36 nm3

SASDAV4 – uPAR wild-type AE105 complex

Urokinase plasminogen activator surface receptorsynthetic peptide AE105 experimental SAS data
Urokinase plasminogen activator surface receptor synthetic peptide AE105 Kratky plot
Sample: Urokinase plasminogen activator surface receptor monomer, 37 kDa Homo sapiens protein
...peptide AE105 monomer, 1 kDa protein
Buffer: 25 mM Sodium Phosphate 5 % Glycerol 50 mM NaSO4, pH: 7.2
Experiment: SAXS data collected at EMBL X33, DORIS III on 2010 Jun 10
A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR). J Biol Chem 287(41):34304-15 (2012)
Mertens HD, Kjaergaard M, Mysling S, Gårdsvoll H, Jørgensen TJ, Svergun DI, Ploug M
RgGuinier 2.5 nm
Dmax 8.5 nm
VolumePorod 61 nm3

SASDAW4 – uPAR wild-type AE234 complex

Urokinase plasminogen activator surface receptorsynthetic peptide AE234 experimental SAS data
Urokinase plasminogen activator surface receptor synthetic peptide AE234 Kratky plot
Sample: Urokinase plasminogen activator surface receptor monomer, 37 kDa Homo sapiens protein
...peptide AE234 monomer, 1 kDa protein
Buffer: 25 mM Sodium Phosphate 5 % Glycerol 50 mM NaSO4, pH: 7.2
Experiment: SAXS data collected at EMBL X33, DORIS III on 2010 Jun 10
A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR). J Biol Chem 287(41):34304-15 (2012)
Mertens HD, Kjaergaard M, Mysling S, Gårdsvoll H, Jørgensen TJ, Svergun DI, Ploug M
RgGuinier 2.4 nm
Dmax 8.3 nm
VolumePorod 57 nm3

SASDG55 – ...peptide, LAP (TGFB-1)

Latency associated peptide experimental SAS data
Latency associated peptide Kratky plot
Sample: ...peptide dimer, 58 kDa Homo sapiens protein
Buffer: phosphate buffered saline 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Apr 20
...peptide between transforming growth factor β-1 bound and unbound states IUCrJ 7(2) (2020)
Stachowski T, Snell M, Snell E
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 129 nm3

SASDG85 – ...peptide complex bound to the CYP7A1 promoter oligonucleotide duplex.

Liver Receptor Homolog-1Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 AlphaCYP7A1 Promoter ForwardCYP7A1 Promoter Reverse experimental SAS data
Liver Receptor Homolog-1 Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 Alpha CYP7A1 Promoter Forward CYP7A1 Promoter Reverse Kratky plot
Sample: Liver Receptor Homolog-1 monomer, 64 kDa Homo sapiens protein
Peroxisome Proliferator-Activated Receptor Gamma Coactivator-1 Alpha monomer, 2 kDa Homo sapiens protein
CYP7A1 Promoter Forward monomer, 4 kDa Homo sapiens DNA
CYP7A1 Promoter Reverse monomer, 4 kDa Homo sapiens DNA
Buffer: 20 mM TRIS, 150 mM NaCl, 2% v/v glycerol, 0.5 mM CHAPS, 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 26
Integrated Structural Modeling of Full-Length LRH-1 Reveals Inter-domain Interactions Contribute to Receptor Structure and Function. Structure (2020)
Seacrist CD, Kuenze G, Hoffmann RM, Moeller BE, Burke JE, Meiler J, Blind RD
RgGuinier 3.8 nm
Dmax 13.0 nm
VolumePorod 76 nm3

SASDGB5 – ...peptide

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM RRESEI, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 3.0 nm
Dmax 13.1 nm
VolumePorod 32 nm3

SASDGC5 – ...peptide (diluted)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 5 mM RRESEI, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.6 nm
Dmax 12.4 nm
VolumePorod 32 nm3

SASDGD5 – ...peptide (Paused SEC)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM RRESEI, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jan 26
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.3 nm
Dmax 6.8 nm
VolumePorod 28 nm3

SASDGE5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.4 nm
Dmax 9.2 nm
VolumePorod 32 nm3

SASDGF5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) (diluted)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 11
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.5 nm
Dmax 9.5 nm
VolumePorod 32 nm3

SASDGG5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) (Paused SEC)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jan 26
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.4 nm
Dmax 6.4 nm
VolumePorod 31 nm3

SASDGH5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM GSH, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Sep 16
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.7 nm
Dmax 6.3 nm
VolumePorod 29 nm3

SASDGJ5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH) (diluted)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 16 mM GSH, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Sep 16
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 3.1 nm
Dmax 7.0 nm
VolumePorod 41 nm3

SASDGK5 – The PDZ1-2 domain of postsynaptic density protein 95 (PSD-95) + glutathione (GSH) (Paused SEC)

PDZ1-2 fragment of PSD-95/Disks large homolog 4 experimental SAS data
OTHER model
Sample: PDZ1-2 fragment of PSD-95/Disks large homolog 4 monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM TRIS/HCl, 150 mM NaCl + 10 mM GSH, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jan 26
...peptide ligand Biophysical Journal (2020)
Rodzli N, Lockhart-Cairns M, Levy C, Chipperfield J, Bird L, Baldock C, Prince S
RgGuinier 2.4 nm
Dmax 7.2 nm
VolumePorod 30 nm3

SASDHQ5 – ...peptide self-assembly

Ile-Leu-Gln-Ile-Asn-Ser peptide experimental SAS data
OTHER model
Sample: ...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

SASDA66 – BAZ2B-18mer complex in Tris

Bromodomain adjacent to zinc finger domain protein 2B, C-terminalH3Kac9Kac14 experimental SAS data
Bromodomain adjacent to zinc finger domain protein 2B, C-terminal H3Kac9Kac14 Kratky plot
Sample: Bromodomain adjacent to zinc finger domain protein 2B, C-terminal monomer, 28 kDa Homo sapiens protein
H3Kac9Kac14 monomer, 5 kDa Homo sapiens protein
Buffer: 20 mM Tris 500 mM NaCl 2 mM DTT 10 microM ZnCl2, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III on 2012 Sep 24
Molecular basis of histone tail recognition by human TIP5 PHD finger and bromodomain of the chromatin remodeling complex NoRC. Structure 23(1):80-92 (2015)
Tallant C, Valentini E, Fedorov O, Overvoorde L, Ferguson FM, Filippakopoulos P, Svergun DI, Knapp S, Ciulli A
RgGuinier 4.2 nm
Dmax 16.0 nm
VolumePorod 52 nm3

SASDJS6 – ...peptide [(POG)10]3

Collagenous Peptide model [(PPG)10]Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD)) experimental SAS data
DAMFILT model
Sample: ...Peptide model [(PPG)10] trimer, 9 kDa synthetic construct protein
Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD)) monomer, 23 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Dec 12
Aromatic residues, Tyr780, His782, Tyr796, Tyr801, located on PKD2 domain of Hathewaya histolytica collagenase, ColH, are involved in the 10-fold enhancement of binding affinity for the enzyme towards...
Perry Caviness
RgGuinier 3.5 nm
Dmax 14.5 nm
VolumePorod 41 nm3

SASDJT6 – ...peptide

Collagen like-peptide [GPRG(POG)13]Collagenase ColH (Polycystic kidney disease 1 (PKD1), Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr689Ser, Phe712Ser, Tyr780Ser, His782Ser, Tyr796Ser and Tyr801) experimental SAS data
DAMFILT model
Sample: ...peptide [GPRG(POG)13] trimer, 11 kDa protein
Collagenase ColH (Polycystic kidney disease 1 (PKD1), Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr689Ser, Phe712Ser, Tyr780Ser, His782Ser, Tyr796Ser and Tyr801) monomer, 33 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 5
Aromatic residues, Tyr780, His782, Tyr796, Tyr801, located on PKD2 domain of Hathewaya histolytica collagenase, ColH, are involved in the 10-fold enhancement of binding affinity for the enzyme towards...
Perry Caviness
RgGuinier 4.0 nm
Dmax 22.0 nm
VolumePorod 61 nm3

SASDJV6 – ...peptide

Collagen like-peptide [GPRG(POG)13]Collagenase ColH (Polycystic kidney disease 1 (PKD1), Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr689Ser and Phe712Ser) experimental SAS data
DAMFILT model
Sample: ...peptide [GPRG(POG)13] trimer, 11 kDa protein
Collagenase ColH (Polycystic kidney disease 1 (PKD1), Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr689Ser and Phe712Ser) monomer, 33 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Dec 12
Aromatic residues, Tyr780, His782, Tyr796, Tyr801, located on PKD2 domain of Hathewaya histolytica collagenase, ColH, are involved in the 10-fold enhancement of binding affinity for the enzyme towards...
Perry Caviness
RgGuinier 4.4 nm
Dmax 21.0 nm
VolumePorod 79 nm3

SASDJX6 – ...peptide

Collagen like-peptide [GPRG(POG)13]Collagenase ColH (Polycystic kidney disease 1 (PKD1), Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD)) experimental SAS data
DAMFILT model
Sample: ...peptide [GPRG(POG)13] trimer, 11 kDa protein
Collagenase ColH (Polycystic kidney disease 1 (PKD1), Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD)) monomer, 34 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 5
Aromatic residues, Tyr780, His782, Tyr796, Tyr801, located on PKD2 domain of Hathewaya histolytica collagenase, ColH, are involved in the 10-fold enhancement of binding affinity for the enzyme towards...
Perry Caviness
RgGuinier 4.0 nm
Dmax 22.0 nm
VolumePorod 63 nm3

SASDJ27 – ...peptide

Collagen like-peptide [GPRG(POG)13]Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr780Ser, His782Ser, Tyr796Ser and Tyr801Ser) experimental SAS data
DAMFILT model
Sample: ...peptide [GPRG(POG)13] trimer, 11 kDa protein
Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD) with Tyr780Ser, His782Ser, Tyr796Ser and Tyr801Ser) monomer, 23 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 5
Aromatic residues, Tyr780, His782, Tyr796, Tyr801, located on PKD2 domain of Hathewaya histolytica collagenase, ColH, are involved in the 10-fold enhancement of binding affinity for the enzyme towards...
Perry Caviness
RgGuinier 3.2 nm
Dmax 18.0 nm
VolumePorod 34 nm3

SASDJ37 – ...peptide

Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD))Collagen like-peptide [GPRG(POG)13] experimental SAS data
DAMFILT model
Sample: Collagenase ColH (Polycystic kidney disease domain 2 (PKD2) and Collagen binding domain (CBD)) monomer, 23 kDa Hathewaya histolytica protein
...peptide [GPRG(POG)13] trimer, 11 kDa protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 5
Aromatic residues, Tyr780, His782, Tyr796, Tyr801, located on PKD2 domain of Hathewaya histolytica collagenase, ColH, are involved in the 10-fold enhancement of binding affinity for the enzyme towards...
Perry Caviness
RgGuinier 3.3 nm
Dmax 18.0 nm
VolumePorod 35 nm3

SASDAE8 – ...peptide

Human Filamin A Ig-like domains 20-21/migfilin peptide complex experimental SAS data
Human Filamin A Ig-like domains 20-21/migfilin peptide complex Kratky plot
Sample: ...peptide complex monomer, 21 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
...Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 2.4 nm
Dmax 8.2 nm
VolumePorod 31 nm3

SASDAF8 – Human Filamin A Ig-like domains 20-21 truncation (2151-2329)

Human Filamin A Ig-like domains 20-21 experimental SAS data
Human Filamin A Ig-like domains 20-21 Kratky plot
Sample: Human Filamin A Ig-like domains 20-21 monomer, 19 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
...Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 2.4 nm
Dmax 8.5 nm
VolumePorod 29 nm3

SASDAG8 – ...peptide

Human Filamin A Ig-like domains 20-21*/migfilin peptide complex experimental SAS data
Human Filamin A Ig-like domains 20-21*/migfilin peptide complex Kratky plot
Sample: ...peptide complex monomer, 23 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
...Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 2.4 nm
Dmax 8.2 nm
VolumePorod 33 nm3

SASDAH8 – Human Filamin A Ig-like domains 20-21* truncation (2141-2329)

Human Filamin A Ig-like domains 20-21* experimental SAS data
DAMMIF model
Sample: Human Filamin A Ig-like domains 20-21* monomer, 20 kDa Homo sapiens protein
Buffer: 20 mM Tris 50 mM NaCl 10mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2014 Feb 1
...Peptide-Bound Filamin A Mechanosensor Domain Pair 20-21. PLoS One 10(8):e0136969 (2015)
Seppälä J, Tossavainen H, Rodic N, Permi P, Pentikäinen U, Ylänne J
RgGuinier 1.9 nm
Dmax 6.8 nm
VolumePorod 32 nm3

SASDHK8 – ...peptide self-assembly (2019-dataset)

Ile-Leu-Gln-Ile-Asn-Ser peptide experimental SAS data
Ile-Leu-Gln-Ile-Asn-Ser peptide Kratky plot
Sample: ...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

SASDDT8 – ...peptide 5 (DILP5)

Insulin-like peptide 5Neural/ectodermal development factor IMP-L2 experimental SAS data
Insulin-like peptide 5 Neural/ectodermal development factor IMP-L2 Kratky plot
Sample: ...peptide 5 monomer, 5 kDa Drosophila melanogaster protein
Neural/ectodermal development factor IMP-L2 monomer, 30 kDa Drosophila melanogaster protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at ID14-3, ESRF on 2011 Nov 20
Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones. Nat Commun 9(1):3860 (2018)
Roed NK, Viola CM, Kristensen O, Schluckebier G, Norrman M, Sajid W, Wade JD, Andersen AS, Kristensen C, Ganderton TR, Turkenburg JP, De Meyts P, Brzozowski AM
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 55 nm3

SASDCW8 – ...peptide @ 4mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunit experimental SAS data
PDB model
Sample: Mitotic spindle assembly checkpoint protein MAD2B monomer, 24 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM EDTA, 10 mM DTT, 5% glycerol, pH: 8.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.1 nm
Dmax 6.5 nm
VolumePorod 46 nm3

SASDCX8 – ...peptide @ 6mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunit experimental SAS data
PDB model
Sample: Mitotic spindle assembly checkpoint protein MAD2B monomer, 24 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM EDTA, 10 mM DTT, 5% glycerol, pH: 8.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.1 nm
Dmax 7.6 nm
VolumePorod 47 nm3

SASDCY8 – ...peptide @ 8mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunit experimental SAS data
PDB model
Sample: Mitotic spindle assembly checkpoint protein MAD2B monomer, 24 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM EDTA, 10 mM DTT, 5% glycerol, pH: 8.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.1 nm
Dmax 7.5 nm
VolumePorod 46 nm3

SASDCZ8 – ...peptide @ 12.2 mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.8 nm

SASDC29 – ...peptide @ 10.6 mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
HADDOCK model
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.9 nm
Dmax 11.0 nm
VolumePorod 108 nm3

SASDC39 – ...peptide @ 9.1mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
HADDOCK model
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 3.0 nm
Dmax 11.4 nm
VolumePorod 107 nm3

SASDC49 – ...peptide @ 6.1mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 3.1 nm
Dmax 11.6 nm
VolumePorod 105 nm3

SASDC59 – ...peptide @ 7.6mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.9 nm
Dmax 11.1 nm
VolumePorod 106 nm3

SASDC69 – ...peptide @ 4.6mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.9 nm

SASDC79 – ...peptide @ 3.0mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.8 nm

SASDC89 – ...peptide @ 1.5 mg/mL

Mitotic spindle assembly checkpoint protein MAD2BDNA polymerase zeta catalytic subunitDNA polymerase zeta catalytic subunit experimental SAS data
Mitotic spindle assembly checkpoint protein MAD2B DNA polymerase zeta catalytic subunit DNA polymerase zeta catalytic subunit Kratky plot
Sample: Mitotic spindle assembly checkpoint protein MAD2B dimer, 49 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
DNA polymerase zeta catalytic subunit monomer, 3 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 10 mM DTT, 5% glycerol, pH: 8
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 May 14
Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex. Proc Natl Acad Sci U S A 115(35):E8191-E8200 (2018)
Rizzo AA, Vassel FM, Chatterjee N, D'Souza S, Li Y, Hao B, Hemann MT, Walker GC, Korzhnev DM
RgGuinier 2.7 nm

SASDHU5 – Heat shock protein 70 (PfHSP70-1)

Heat shock protein 70Peptide experimental SAS data
DAMFILT model
Sample: Heat shock protein 70 monomer, 74 kDa Plasmodium falciparum protein
Peptide monomer, 1 kDa synthetic construct protein
Buffer: 50mM Tris, 5mM MgCl2, 500mM KCl, 5mM Bme, 5% glycerol, pH: 8
Experiment: SAXS data collected at Anton Paar SAXSpace, CSIR-Central Drug Research Institute on 2019 Oct 24
Structural-functional diversity of malaria parasite's PfHSP70-1 and PfHSP40 chaperone pair gives an edge over human orthologs in chaperone-assisted protein folding. Biochem J 477(18):3625-3643 (2020)
Anas M, Shukla A, Tripathi A, Kumari V, Prakash C, Nag P, Kumar LS, Sharma SK, Ramachandran R, Kumar N
RgGuinier 5.3 nm
Dmax 16.6 nm
VolumePorod 450 nm3