Small Angle Scattering Biological Data Bank SASBDB

Browse by ORGANISM: Escherichia coli

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

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

SASDA55 – Nucleoplasmin

Sample:	Nucleoplasmin pentamer, 110 kDa Escherichia coli protein
Buffer:	20 mM Pipes buffer 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Dec 3

A mechanism for histone chaperoning activity of nucleoplasmin: thermodynamic and structural models. J Mol Biol 393(2):448-63 (2009)
Taneva SG, Bañuelos S, Falces J, Arregi I, Muga A, Konarev PV, Svergun DI, Velázquez-Campoy A, Urbaneja MA

R_g^Guinier	4.0	nm
D_max	12.6	nm
Volume^Porod	210	nm³

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