Browse by MODEL: Hybrid

SASDFL7 – Complex with 1H histone chaperone Asf1, histones H3 and H4, 2H acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) in 42% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-length experimental SAS data
GROMACS model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14
Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 3.4 nm
Dmax 10.5 nm

SASDFM7 – Complex with 1H histone chaperone Asf1, histones H3 and H4, acetylatransferase Rtt109, 2H histone chaperone Vps75 (1-225aa) in 42% v/v D2O

Vacuolar protein sorting-associated protein 75 (1-225 aa)Histone acetyltransferase RTT109Histone chaperone ASF1Histone H4Histone H3 full-length experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Vacuolar protein sorting-associated protein 75 (1-225 aa) dimer, 53 kDa Saccharomyces cerevisiae protein
Histone acetyltransferase RTT109 monomer, 50 kDa Saccharomyces cerevisiae protein
Histone chaperone ASF1 monomer, 19 kDa protein
Histone H4 monomer, 11 kDa Xenopus laevis protein
Histone H3 full-length monomer, 15 kDa Xenopus laevis protein
Buffer: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O, pH: 6.5
Experiment: SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 14
Histone chaperone exploits intrinsic disorder to switch acetylation specificity (Asf1-H3:H4-Rtt109-Vps75 protein complex, data for docking block selections) Nat Commun 10(1):3435 (2019)
Danilenko N, Lercher L, Kirkpatrick J, Gabel F, Codutti L, Carlomagno T
RgGuinier 2.7 nm
Dmax 9.0 nm

SASDES6 – The 11S subunit of the Plasmodium falciparum proteasome, PA28

Proteasome activator PA28 experimental SAS data
CORAL model
Sample: Proteasome activator PA28 heptamer, 232 kDa Plasmodium falciparum protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, 0.5 mM TCEP, 0.1% sodium azide, pH: 7.4
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Dec 2
The structure of the PA28-20S proteasome complex from Plasmodium falciparum and implications for proteostasis. Nat Microbiol 4(11):1990-2000 (2019)
Xie SC, Metcalfe RD, Hanssen E, Yang T, Gillett DL, Leis AP, Morton CJ, Kuiper MJ, Parker MW, Spillman NJ, Wong W, Tsu C, Dick LR, Griffin MDW, Tilley L
RgGuinier 4.3 nm
Dmax 12.9 nm
VolumePorod 484 nm3

SASDEV6 – KRAB-associated protein 1 (KAP1); TRIM28; full length protein

Transcription intermediary factor 1-beta, TIF1b, KAP1, TRIM28 experimental SAS data
GASBOR model
Sample: Transcription intermediary factor 1-beta, TIF1b, KAP1, TRIM28 dimer, 183 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 500 mM NaCl, 10 % Glycerol, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Jul 6
KAP1 is an antiparallel dimer with a functional asymmetry. Life Sci Alliance 2(4) (2019)
Fonti G, Marcaida MJ, Bryan LC, Träger S, Kalantzi AS, Helleboid PJ, Demurtas D, Tully MD, Grudinin S, Trono D, Fierz B, Dal Peraro M
RgGuinier 9.0 nm
Dmax 38.0 nm
VolumePorod 710 nm3

SASDEW6 – KRAB-associated protein 1, (KAP1); TRIM28; 23-418 RBCC domain

Transcription intermediary factor 1-beta, TIF1b, KAP1, TRIM28, Fragment 23-418, RBCC domain experimental SAS data
GASBOR model
Sample: Transcription intermediary factor 1-beta, TIF1b, KAP1, TRIM28, Fragment 23-418, RBCC domain dimer, 92 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 500 mM NaCl, 10 % Glycerol, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2017 Jul 6
KAP1 is an antiparallel dimer with a functional asymmetry. Life Sci Alliance 2(4) (2019)
Fonti G, Marcaida MJ, Bryan LC, Träger S, Kalantzi AS, Helleboid PJ, Demurtas D, Tully MD, Grudinin S, Trono D, Fierz B, Dal Peraro M
RgGuinier 8.3 nm
Dmax 37.0 nm
VolumePorod 381 nm3

SASDFD3 – Filamin A Ig-like domains 4-6 (FLNa4-6)

Filamin A Ig-like domains 4-6 experimental SAS data
DAMFILT model
Sample: Filamin A Ig-like domains 4-6 monomer, 32 kDa Homo sapiens protein
Buffer: 20 mM Tris, 100 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2017 Feb 10
Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia. Biophys J 117(8):1467-1475 (2019)
Haataja TJK, Capoulade R, Lecointe S, Hellman M, Merot J, Permi P, Pentikäinen U
RgGuinier 2.7 nm
Dmax 9.5 nm
VolumePorod 41 nm3

SASDEK8 – Farnesylated human Guanylate Binding Protein 1 (farn-hGBP1), batch mode

farnesylated human Guanylate-binding protein 1 experimental SAS data
PYMOL model
Sample: Farnesylated human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2016 May 8
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 3.8 nm
Dmax 14.3 nm
VolumePorod 102 nm3

SASDEL8 – Human Guanylate Binding Protein 1 (hGBP1), batch mode

human Guanylate-binding protein 1 experimental SAS data
PYMOL model
Sample: Human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2016 May 8
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 5.1 nm
Dmax 27.4 nm
VolumePorod 162 nm3

SASDEM8 – Human Guanylate Binding Protein 1 with GppNHp (hGBP1 + GppNHp), batch mode

human Guanylate-binding protein 1 experimental SAS data
PYMOL model
Sample: Human Guanylate-binding protein 1 monomer, 69 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 5 mM MgCl2, 150 mM NaCl, 0.2 mM GppNHp, pH: 7.9
Experiment: SAXS data collected at BM29, ESRF on 2016 May 8
Farnesylation of human guanylate binding protein 1 as safety mechanism preventing structural rearrangements and uninduced dimerization. FEBS J (2019)
Lorenz C, Ince S, Zhang T, Cousin A, Batra-Safferling R, Nagel-Steger L, Herrmann C, Stadler AM
RgGuinier 5.5 nm
Dmax 27.0 nm
VolumePorod 186 nm3

SASDF65 – Resistance to inhibitors of cholinesterase 8 homolog A (Ric8a) amino acids 1-492

Resistance to inhibitors of cholinesterase 8 homolog A experimental SAS data
BILBOMD model
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 56 kDa Bos taurus protein
Buffer: 20 mM Tris, 150 mM KCl, 5 % glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Oct 27
Structural underpinnings of Ric8A function as a G-protein α-subunit chaperone and guanine-nucleotide exchange factor. Nat Commun 10(1):3084 (2019)
Srivastava D, Gakhar L, Artemyev NO
RgGuinier 3.4 nm
Dmax 12.7 nm
VolumePorod 88 nm3