Browse by ORGANISM: other species

SASDQK8 – G. gallus TRPV4 N-terminal Domain, deletion mutant ∆N104

Transient receptor potential cation channel subfamily V member 4 experimental SAS data
Transient receptor potential cation channel subfamily V member 4 Kratky plot
Sample: Transient receptor potential cation channel subfamily V member 4 monomer, 32 kDa Gallus gallus protein
Buffer: 20 mM Tris, 300 mM NaCl, 10 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Mar 16
Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity Nature Communications 14(1) (2023)
Goretzki B, Wiedemann C, McCray B, Schäfer S, Jansen J, Tebbe F, Mitrovic S, Nöth J, Cabezudo A, Donohue J, Jeffries C, Steinchen W, Stengel F, Sumner C, Hummer G, Hellmich U
RgGuinier 2.8 nm
Dmax 13.0 nm
VolumePorod 49 nm3

SASDQL8 – G. gallus TRPV4 N-terminal Domain, deletion mutant ∆N120

Transient receptor potential cation channel subfamily V member 4 experimental SAS data
Transient receptor potential cation channel subfamily V member 4 Kratky plot
Sample: Transient receptor potential cation channel subfamily V member 4 monomer, 29 kDa Gallus gallus protein
Buffer: 20 mM Tris, 300 mM NaCl, 10 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Mar 16
Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity Nature Communications 14(1) (2023)
Goretzki B, Wiedemann C, McCray B, Schäfer S, Jansen J, Tebbe F, Mitrovic S, Nöth J, Cabezudo A, Donohue J, Jeffries C, Steinchen W, Stengel F, Sumner C, Hummer G, Hellmich U
RgGuinier 2.7 nm
Dmax 12.5 nm
VolumePorod 43 nm3

SASDQM8 – G. gallus TRPV4 intrinsically disordered N-terminus

Transient receptor potential cation channel subfamily V member 4 experimental SAS data
G. gallus TRPV4 intrinsically disordered N-terminus Rg histogram
Sample: Transient receptor potential cation channel subfamily V member 4 monomer, 15 kDa Gallus gallus protein
Buffer: 20 mM Tris, 100 mM NaCl, 10 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Dec 16
Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity Nature Communications 14(1) (2023)
Goretzki B, Wiedemann C, McCray B, Schäfer S, Jansen J, Tebbe F, Mitrovic S, Nöth J, Cabezudo A, Donohue J, Jeffries C, Steinchen W, Stengel F, Sumner C, Hummer G, Hellmich U
RgGuinier 3.2 nm
Dmax 14.5 nm
VolumePorod 59 nm3

SASDQN8 – G. gallus TRPV4 intrinsically disordered N-terminus, mutation 107-KRWRR-111 to 107-AAWAA-111

Transient receptor potential cation channel subfamily V member 4 experimental SAS data
G. gallus TRPV4 intrinsically disordered N-terminus, mutation 107-KRWRR-111 to 107-AAWAA-111 Rg histogram
Sample: Transient receptor potential cation channel subfamily V member 4 monomer, 14 kDa Gallus gallus protein
Buffer: 20 mM Tris, 100 mM NaCl, 10 mM DTT, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Dec 16
Crosstalk between regulatory elements in disordered TRPV4 N-terminus modulates lipid-dependent channel activity Nature Communications 14(1) (2023)
Goretzki B, Wiedemann C, McCray B, Schäfer S, Jansen J, Tebbe F, Mitrovic S, Nöth J, Cabezudo A, Donohue J, Jeffries C, Steinchen W, Stengel F, Sumner C, Hummer G, Hellmich U
RgGuinier 3.3 nm
Dmax 14.5 nm
VolumePorod 37 nm3

SASDPV7 – FAD-dependent monooxygenase from Stenotrophomonas maltophilia (no reducing agent)

Monooxygenase (M154I, A283T) experimental SAS data
REFMAC model
Sample: Monooxygenase (M154I, A283T) monomer, 39 kDa Stenotrophomonas maltophilia protein
Buffer: 25 mM Bis-Tris, 150 mM NaCl, pH: 6.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Jan 10
Tetracycline-modifying enzyme Sm TetX from Stenotrophomonas maltophilia Acta Crystallographica Section F Structural Biology Communications 79(7):180-192 (2023)
Malý M, Kolenko P, Stránský J, Švecová L, Dušková J, Koval' T, Skálová T, Trundová M, Adámková K, Černý J, Božíková P, Dohnálek J
RgGuinier 2.4 nm
Dmax 6.8 nm
VolumePorod 59 nm3

SASDPW7 – FAD-dependent monooxygenase from Stenotrophomonas maltophilia (with reducing agent)

Monooxygenase (M154I, A283T) experimental SAS data
REFMAC model
Sample: Monooxygenase (M154I, A283T) monomer, 39 kDa Stenotrophomonas maltophilia protein
Buffer: 25 mM Bis-Tris, 150 mM NaCl, 30 mM DTT, pH: 6.5
Experiment: SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Jan 7
Tetracycline-modifying enzyme Sm TetX from Stenotrophomonas maltophilia Acta Crystallographica Section F Structural Biology Communications 79(7):180-192 (2023)
Malý M, Kolenko P, Stránský J, Švecová L, Dušková J, Koval' T, Skálová T, Trundová M, Adámková K, Černý J, Božíková P, Dohnálek J
RgGuinier 2.4 nm
Dmax 6.4 nm
VolumePorod 64 nm3

SASDLK7 – Bartonella effector protein (Bep1), 15 °C

Bartonella effector protein (Bep) substrate of VirB T4SS experimental SAS data
GASBOR model
Sample: Bartonella effector protein (Bep) substrate of VirB T4SS monomer, 64 kDa Bartonella clarridgeiae (strain … protein
Buffer: 25 mM Hepes, 300 mM NaCl, 1 mM TCEP, 5% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at Xenocs Xeuss 2.0 Q-Xoom, Center for Structural Studies, Heinrich-Heine-University on 2020 May 29
Structure and function of Bartonella effector protein 1: target and interdomain interactions University of Basel PhD thesis 15051 (2023)
Markus Huber, Jens Reiners
RgGuinier 4.1 nm
Dmax 13.4 nm
VolumePorod 83 nm3

SASDLL7 – Bartonella effector protein (Bep1), 20 °C

Bartonella effector protein (Bep) substrate of VirB T4SS experimental SAS data
GASBOR model
Sample: Bartonella effector protein (Bep) substrate of VirB T4SS monomer, 64 kDa Bartonella clarridgeiae (strain … protein
Buffer: 25 mM Hepes, 300 mM NaCl, 1 mM TCEP, 5% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 26
Structure and function of Bartonella effector protein 1: target and interdomain interactions University of Basel PhD thesis 15051 (2023)
Markus Huber, Jens Reiners
RgGuinier 3.8 nm
Dmax 13.4 nm
VolumePorod 87 nm3

SASDLM7 – Bartonella effector protein (Bep1), 35 °C

Bartonella effector protein (Bep) substrate of VirB T4SS experimental SAS data
GASBOR model
Sample: Bartonella effector protein (Bep) substrate of VirB T4SS monomer, 64 kDa Bartonella clarridgeiae (strain … protein
Buffer: 25 mM Hepes, 300 mM NaCl, 1 mM TCEP, 5% v/v glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Jun 26
Structure and function of Bartonella effector protein 1: target and interdomain interactions University of Basel PhD thesis 15051 (2023)
Markus Huber, Jens Reiners
RgGuinier 4.1 nm
Dmax 14.4 nm
VolumePorod 108 nm3

SASDRR8 – Сhloroplast FOF1-ATP synthase from Spinacia oleracea purified by anion-exchange chromatography (~ 300 mM NaCl)

ATP synthase subunit alpha, chloroplasticATP synthase subunit beta, chloroplasticATP synthase gamma chain, chloroplasticATP synthase delta chain, chloroplasticATP synthase epsilon chain, chloroplasticATP synthase subunit a, chloroplasticATP synthase subunit b, chloroplasticATP synthase subunit b', chloroplasticATP synthase subunit c, chloroplastic4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside experimental SAS data
MEMPROT model
Sample: ATP synthase subunit alpha, chloroplastic trimer, 166 kDa Spinacia oleracea protein
ATP synthase subunit beta, chloroplastic trimer, 161 kDa Spinacia oleracea protein
ATP synthase gamma chain, chloroplastic monomer, 40 kDa Spinacia oleracea protein
ATP synthase delta chain, chloroplastic monomer, 28 kDa Spinacia oleracea protein
ATP synthase epsilon chain, chloroplastic monomer, 15 kDa Spinacia oleracea protein
ATP synthase subunit a, chloroplastic monomer, 27 kDa Spinacia oleracea protein
ATP synthase subunit b, chloroplastic monomer, 21 kDa Spinacia oleracea protein
ATP synthase subunit b', chloroplastic monomer, 24 kDa Spinacia oleracea protein
ATP synthase subunit c, chloroplastic 14-mer, 112 kDa Spinacia oleracea protein
4-trans-(4-trans-Propylcyclohexyl)-cyclohexyl α-maltoside 0, 283 kDa
Buffer: 300 mM NaCl, 30 mM HEPES, 2 mM MgCl2, 0.04% (w/v) tPCC-α-M, pH: 8
Experiment: SAXS data collected at Rigaku MicroMax 007-HF, Moscow Institute of Physics and Technology (MIPT) on 2020 Oct 3
I-Shaped Dimers of a Plant Chloroplast FOF1-ATP Synthase in Response to Changes in Ionic Strength International Journal of Molecular Sciences 24(13):10720 (2023)
Osipov S, Ryzhykau Y, Zinovev E, Minaeva A, Ivashchenko S, Verteletskiy D, Sudarev V, Kuklina D, Nikolaev M, Semenov Y, Zagryadskaya Y, Okhrimenko I, Gette M, Dronova E, Shishkin A, Dencher N, Kuklin A, Ivanovich V, Uversky V, Vlasov A
RgGuinier 6.6 nm
Dmax 27.5 nm
VolumePorod 927 nm3