Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: Ensemble

SASDEP2 – Unlabeled Nuclear Localization Signal (NLS) from the inner nuclear membrane protein HEH2 with denaturant

Inner nuclear membrane protein HEH2 experimental SAS data

Unlabeled Nuclear Localization Signal (NLS) from the inner nuclear membrane protein HEH2 with denaturant Rg histogram

Sample:	Inner nuclear membrane protein HEH2 monomer, 5 kDa Saccharomyces cerevisiae protein
Buffer:	25 mM HEPES, 150 mM NaCl, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2014 Jan 25

Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA

R_g^Guinier	2.3	nm
D_max	7.1	nm
Volume^Porod	10	nm³

SASDER2 – Unlabeled Importin Beta Binding domain (IBB) from importin subunit alpha-1 without denaturant

Importin subunit alpha-1 experimental SAS data

Unlabeled Importin Beta Binding domain (IBB) from importin subunit alpha-1 without denaturant Rg histogram

Sample:	Importin subunit alpha-1 monomer, 11 kDa Homo sapiens protein
Buffer:	PBS, 10 mM DTT, pH: 7.4
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Dec 8

R_g^Guinier	3.2	nm
D_max	11.5	nm
Volume^Porod	30	nm³

SASDET2 – Unlabeled Importin Beta Binding Domain (IBB) from importin subunit alpha-1 with denaturant

Unlabeled Importin Beta Binding Domain (IBB) from importin subunit alpha-1 with denaturant Rg histogram

Sample:	Importin subunit alpha-1 monomer, 11 kDa Homo sapiens protein
Buffer:	PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Jun 15

R_g^Guinier	3.1	nm
D_max	15.3	nm
Volume^Porod	34	nm³

SASDEV2 – Unlabeled nuclear pore complex protein Nup153 (NUS) without denaturant

Nuclear pore complex protein Nup153 experimental SAS data

Unlabeled nuclear pore complex protein Nup153 (NUS) without denaturant Rg histogram

Sample:	Nuclear pore complex protein Nup153 monomer, 8 kDa Homo sapiens protein
Buffer:	PBS, 10 mM DTT, pH: 7.4
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Nov 8

R_g^Guinier	2.5	nm
D_max	9.2	nm
Volume^Porod	15	nm³

SASDEX2 – Unlabeled nuclear pore complex protein Nup153 (NUS) with denaturant

Unlabeled nuclear pore complex protein Nup153 (NUS) with denaturant Rg histogram

Sample:	Nuclear pore complex protein Nup153 monomer, 8 kDa Homo sapiens protein
Buffer:	PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Jun 15

R_g^Guinier	3.1	nm
D_max	11.0	nm
Volume^Porod	26	nm³

SASDEZ2 – Unlabeled nuclear pore complex protein Nup153 (NUL) without denaturant

Unlabeled nuclear pore complex protein Nup153 (NUL) without denaturant Rg histogram

Sample:	Nuclear pore complex protein Nup153 monomer, 12 kDa Homo sapiens protein
Buffer:	PBS, 10 mM DTT, pH: 7.4
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Nov 8

R_g^Guinier	3.0	nm
D_max	10.9	nm
Volume^Porod	32	nm³

SASDE33 – Unlabeled nuclear pore complex protein Nup153 (NUL) with denaturant

Unlabeled nuclear pore complex protein Nup153 (NUL) with denaturant Rg histogram

Sample:	Nuclear pore complex protein Nup153 monomer, 12 kDa Homo sapiens protein
Buffer:	PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Nov 8

R_g^Guinier	3.5	nm
D_max	16.0	nm
Volume^Porod	53	nm³

SASDBW6 – Suppressor of Copper Sensitivity C protein (ScsC) from P. mirabilis (mutant)

Suppressor of Copper Sensitivity C protein (mutant) experimental SAS data

Suppressor of Copper Sensitivity C protein (ScsC) from P. mirabilis (mutant) Rg histogram

Sample:	Suppressor of Copper Sensitivity C protein (mutant) trimer, 73 kDa Proteus mirabilis protein
Buffer:	25 mM HEPES 150mM NaCl, 1mM DTT,, pH: 7.5
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Jul 22

A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance. Nat Commun 8:16065 (2017)
Furlong EJ, Lo AW, Kurth F, Premkumar L, Totsika M, Achard MES, Halili MA, Heras B, Whitten AE, Choudhury HG, Schembri MA, Martin JL

R_g^Guinier	4.4	nm
D_max	13.5	nm
Volume^Porod	108	nm³

SASDB94 – Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis

C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein experimental SAS data

Suppressor of Copper Sensitivity C protein (ScsC) from Proteus mirabilis Rg histogram

Sample:	C-terminal catalytic domain of Suppressor of Copper Sensitivity C protein monomer, 20 kDa Proteus mirabilis protein
Buffer:	25 mM HEPES 150mM NaCl 1mM DTT, pH: 7.5
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2012 Feb 29

R_g^Guinier	3.7	nm
D_max	10.5	nm
Volume^Porod	92	nm³

SASDB45 – Trimeric periplasmic holdase chaperone protein Skp

Periplasmic holdase chaperone protein Skp experimental SAS data

Trimeric periplasmic holdase chaperone protein Skp Rg histogram

Sample:	Periplasmic holdase chaperone protein Skp trimer, 47 kDa Escherichia coli protein
Buffer:	25 mM HEPES 150 mM NaCl 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Sep 24

A Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperone. Structure 25(7):1079-1088.e3 (2017)
Holdbrook DA, Burmann BM, Huber RG, Petoukhov MV, Svergun DI, Hiller S, Bond PJ

R_g^Guinier	3.6	nm
D_max	12.8	nm
Volume^Porod	168	nm³

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