Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: Ab initio only

SASDMY2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox experimental SAS data

Sample:	Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) without Dox monomer, 125 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19

Hydrolytically degradable polymer micelles for drug delivery: a SAXS/SANS kinetic study. Biomacromolecules 14(11):4061-70 (2013)
Filippov SK, Franklin JM, Konarev PV, Chytil P, Etrych T, Bogomolova A, Dyakonova M, Papadakis CM, Radulescu A, Ulbrich K, Stepanek P, Svergun DI

R_g^Guinier	6.5	nm
D_max	22.9	nm

SASDMZ2 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%) experimental SAS data

Sample:	Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - Lev-Chol) with Dox (10%) monomer, 125 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19

R_g^Guinier	6.9	nm
D_max	23.8	nm

SASDM23 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox experimental SAS data

Sample:	Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) without Dox monomer, 125 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 16

R_g^Guinier	5.9	nm
D_max	19.7	nm

SASDM33 – Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%)

Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%) experimental SAS data

Sample:	Hydrolytically Degradable Polymer Micelles for Drug Delivery (structure of hydrophobic substituent - cholest-4-en-3-one) with Dox (10%) monomer, 125 kDa
Buffer:	phosphate buffer saline (PBS) (pH 5.0), pH: 5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2012 Aug 19

R_g^Guinier	5.5	nm
D_max	18.3	nm

SASDAS4 – I27-PimA

I27-PimA Fusion protein experimental SAS data

Sample:	I27-PimA Fusion protein monomer, 48 kDa protein
Buffer:	50 mM Tris-HCl 150 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2014 May 17

Conformational plasticity of the essential membrane-associated mannosyltransferase PimA from mycobacteria. J Biol Chem 288(41):29797-808 (2013)
Giganti D, Alegre-Cebollada J, Urresti S, Albesa-Jové D, Rodrigo-Unzueta A, Comino N, Kachala M, López-Fernández S, Svergun DI, Fernández JM, Guerin ME

R_g^Guinier	3.1	nm
D_max	10.7	nm
Volume^Porod	86	nm³

SASDMZ4 – Mixture of estrogen-related receptor gamma:Inverse repeat IR3 DNA - 6:3 and 2:1 complexes - at 2.9 mg/ml

Estrogen-related receptor gammaInverse repeat IR3 DNA experimental SAS data

Sample:	Estrogen-related receptor gamma hexamer, 230 kDa Homo sapiens protein Inverse repeat IR3 DNA trimer, 46 kDa DNA
Buffer:	20 mM Tris-HCl, 100 mM NaCl, 100 mM KCl, 5 mM MgCl2, 1% (v/v) glycerol, and 1 mM CHAPS, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Mar 3

Reconstruction of Quaternary Structure from X-ray Scattering by Equilibrium Mixtures of Biological Macromolecules Biochemistry 52(39):6844-6855 (2013)
Petoukhov M, Billas I, Takacs M, Graewert M, Moras D, Svergun D

R_g^Guinier	4.7	nm
D_max	14.6	nm

SASDM25 – Mixture of estrogen-related receptor gamma:Inverse repeat IR3 DNA - 6:3 and 2:1 complexes - at 1.9 mg/ml

Sample:	Estrogen-related receptor gamma hexamer, 230 kDa Homo sapiens protein Inverse repeat IR3 DNA trimer, 46 kDa DNA
Buffer:	20 mM Tris-HCl, 100 mM NaCl, 100 mM KCl, 5 mM MgCl2, 1% (v/v) glycerol, and 1 mM CHAPS, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Mar 3

R_g^Guinier	4.3	nm
D_max	13.2	nm

SASDM35 – Mixture of estrogen-related receptor gamma:Inverse repeat IR3 DNA - 6:3 and 2:1 complexes - at 1.0 mg/ml

Sample:	Estrogen-related receptor gamma hexamer, 230 kDa Homo sapiens protein Inverse repeat IR3 DNA trimer, 46 kDa DNA
Buffer:	20 mM Tris-HCl, 100 mM NaCl, 100 mM KCl, 5 mM MgCl2, 1% (v/v) glycerol, and 1 mM CHAPS, pH: 8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Mar 3

R_g^Guinier	4.1	nm
D_max	12.8	nm

SASDAN3 – MutS dimer

DNA mismatch repair protein MutS experimental SAS data

Sample:	DNA mismatch repair protein MutS dimer, 191 kDa Escherichia coli protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Feb 28

Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res 41(17):8166-81 (2013)
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK

R_g^Guinier	4.7	nm
D_max	15.5	nm
Volume^Porod	307	nm³

SASDAQ3 – MutS tetramer

Sample:	DNA mismatch repair protein MutS tetramer, 381 kDa Escherichia coli protein
Buffer:	50 mM HEPES 50 mM KCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 12

R_g^Guinier	7.8	nm
D_max	28.0	nm
Volume^Porod	700	nm³

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