Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: Hybrid

SASDAC5 – ImportinA_ImportinB

ImportinA_ImportinB experimental SAS data

Sample:	ImportinA_ImportinB monomer, 160 kDa Escherichia coli protein
Buffer:	50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Oct 29

Recognition of nucleoplasmin by its nuclear transport receptor importin α/β: insights into a complete import complex. Biochemistry 49(45):9756-69 (2010)
Falces J, Arregi I, Konarev PV, Urbaneja MA, Svergun DI, Taneva SG, Bañuelos S

R_g^Guinier	5.7	nm
D_max	19.0	nm
Volume^Porod	390	nm³

SASDAD5 – Nucleoplasmin_ImpA_ImpB

Nucleoplasmin_importinA_importinB experimental SAS data

Sample:	Nucleoplasmin_importinA_importinB, 900 kDa Escherichia coli protein
Buffer:	50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2008 May 23

R_g^Guinier	8.6	nm
D_max	28.0	nm
Volume^Porod	1800	nm³

SASDAV6 – Cysteine desulfurase IscS dimer

Cysteine desulfurase IscS experimental SAS data

Sample:	Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein
Buffer:	20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5

Structural bases for the interaction of frataxin with the central components of iron-sulphur cluster assembly. Nat Commun 1:95 (2010)
Prischi F, Konarev PV, Iannuzzi C, Pastore C, Adinolfi S, Martin SR, Svergun DI, Pastore A

R_g^Guinier	3.2	nm
D_max	10.9	nm

SASDAW6 – Iron-sulfur cluster assembly scaffold IscU monomer

Iron-sulfur cluster assembly scaffold protein IscU experimental SAS data

Sample:	Iron-sulfur cluster assembly scaffold protein IscU monomer, 14 kDa Escherichia coli protein
Buffer:	20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5

R_g^Guinier	1.9	nm
D_max	6.4	nm

SASDAX6 – Protein CyaY monomer

Sample:	Protein CyaY monomer, 12 kDa Escherichia coli protein
Buffer:	20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5

R_g^Guinier	1.5	nm
D_max	5.0	nm

SASDAY6 – IcsS-dimer and IscU-dimer complex

Cysteine desulfurase IscSIron-sulfur cluster assembly scaffold protein IscU experimental SAS data

Sample:	Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein Iron-sulfur cluster assembly scaffold protein IscU dimer, 29 kDa Escherichia coli protein
Buffer:	20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5

R_g^Guinier	3.6	nm
D_max	12.1	nm

SASDAZ6 – CyaY-dimer and IscS-dimer complex

Cysteine desulfurase IscSProtein CyaY experimental SAS data

Sample:	Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein Protein CyaY dimer, 24 kDa Escherichia coli protein
Buffer:	20 mM Tris-HCl, 50 mM NaCl, 10 mM β-mercaptoethanol and ferrous ammonium sulphate, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5

R_g^Guinier	3.1	nm
D_max	10.9	nm

SASDA27 – IcsS, IscU and CyaY dimeric complex

Cysteine desulfurase IscSIron-sulfur cluster assembly scaffold protein IscUProtein CyaY experimental SAS data

Sample:	Cysteine desulfurase IscS dimer, 87 kDa Escherichia coli protein Iron-sulfur cluster assembly scaffold protein IscU dimer, 29 kDa Escherichia coli protein Protein CyaY dimer, 24 kDa Escherichia coli protein
Buffer:	20 mM Tris-HCl 150 mM NaCl 10 mM β-mercaptoethanol, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 5

R_g^Guinier	3.5	nm
D_max	11.9	nm

SASDC56 – Blue light receptor YtvA, dark/inactive state

pfyP - Blue light photoreceptor experimental SAS data

Sample:	PfyP - Blue light photoreceptor dimer, 58 kDa Bacillus subtilis protein
Buffer:	PBS + 5 mM DTT, pH: 7.4
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Oct 24

The switch that does not flip: the blue-light receptor YtvA from Bacillus subtilis adopts an elongated dimer conformation independent of the activation state as revealed by a combined AUC and SAXS study. J Mol Biol 403(1):78-87 (2010)
Jurk M, Dorn M, Kikhney A, Svergun D, Gärtner W, Schmieder P

R_g^Guinier	3.2	nm
D_max	10.1	nm
Volume^Porod	75	nm³

SASDCN3 – Phosphoenolpyruvate-protein phosphotransferase

Phosphoenolpyruvate-protein phosphotransferase experimental SAS data

Sample:	Phosphoenolpyruvate-protein phosphotransferase dimer, 127 kDa Escherichia coli protein
Buffer:	20mM TRIS buffer, 100 mM NaCl, 10 mM DTT, 4 mM MgCl2, 1 mM EDTA, pH: 7.4
Experiment:	SAXS data collected at 12-ID-C, Advanced Photon Source (APS), Argonne National Laboratory on 2010 Aug 23

Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering. J Am Chem Soc 132(37):13026-45 (2010)
Schwieters CD, Suh JY, Grishaev A, Ghirlando R, Takayama Y, Clore GM

R_g^Guinier	4.1	nm
D_max	14.8	nm
Volume^Porod	189	nm³

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