Small Angle Scattering Biological Data Bank SASBDB

Browse by MACROMOLECULE type: protein

SASDC66 – Blue light receptor YtvA, lit/active 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	74	nm³

SASDD35 – Nanodiscs with membrane scaffold protein 1D1 (MSP1D1) and dilaurylphosphatidyl choline (DLPC)

Membrane scaffold protein 1D1 experimental SAS data

Sample:	Membrane scaffold protein 1D1 dimer, 50 kDa unidentified protein
Buffer:	20 mM Tris, 100 mM NaCl, 100 mM sodium cholate,, pH: 7.4
Experiment:	SAXS data collected at ID14-3, ESRF on 2009 Nov 14

Elliptical structure of phospholipid bilayer nanodiscs encapsulated by scaffold proteins: casting the roles of the lipids and the protein. J Am Chem Soc 132(39):13713-22 (2010)
Skar-Gislinge N, Simonsen JB, Mortensen K, Feidenhans'l R, Sligar SG, Lindberg Møller B, Bjørnholm T, Arleth L

R_g^Guinier	4.9	nm
D_max	12.2	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

SASDMN9 – Conformational characterization of A77-78 fibronectin type III tandem

Sample:	Titin monomer, 22 kDa Homo sapiens protein
Buffer:	100 mM NaCl, 50 mM Tris-HCl, 2mM DTT, pH: 7.2
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Jul 3

The Structure of the FnIII Tandem A77-A78 Points to a Periodically Conserved Architecture in the Myosin-Binding Region of Titin Journal of Molecular Biology 401(5):843-853 (2010)
Bucher R, Svergun D, Muhle-Goll C, Mayans O

R_g^Guinier	2.5	nm
D_max	90.0	nm
Volume^Porod	21	nm³

SASDMP9 – Conformational characterization of A80-82 fibronectin type III tandem

Sample:	Titin monomer, 32 kDa Homo sapiens protein
Buffer:	100 mM NaCl, 50 mM Tris-HCl, 2mM DTT, pH: 7.2
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Jul 3

R_g^Guinier	3.7	nm
D_max	130.0	nm
Volume^Porod	39	nm³

SASDMQ9 – Conformational characterization of A84-86 fibronectin type III tandem

Sample:	Titin monomer, 32 kDa Homo sapiens protein
Buffer:	100 mM NaCl, 50 mM Tris-HCl, 2mM DTT, pH: 7.2
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Oct 6

R_g^Guinier	3.7	nm
D_max	14.0	nm

SASDAY4 – fH1015

Factor H CCP modules 10 to 15 experimental SAS data

Sample:	Factor H CCP modules 10 to 15 monomer, 41 kDa Homo sapiens protein
Buffer:	50 mM Potassium Phosphate, pH: 7.4
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Dec 2

The central portion of factor H (modules 10-15) is compact and contains a structurally deviant CCP module. J Mol Biol 395(1):105-22 (2010)
Schmidt CQ, Herbert AP, Mertens HD, Guariento M, Soares DC, Uhrin D, Rowe AJ, Svergun DI, Barlow PN

R_g^Guinier	3.0	nm
D_max	10.4	nm
Volume^Porod	68	nm³

SASDAZ4 – fH1114

Factor H CCP modules 11 to 14 experimental SAS data

Sample:	Factor H CCP modules 11 to 14 monomer, 28 kDa Homo sapiens protein
Buffer:	50 mM Potassium Phosphate, pH: 7.4
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Dec 2

R_g^Guinier	3.0	nm
D_max	10.5	nm
Volume^Porod	38	nm³

SASDA25 – fh1213

Factor H CCP modules 12 to 13 experimental SAS data

Sample:	Factor H CCP modules 12 to 13 monomer, 14 kDa Homo sapiens protein
Buffer:	50 mM Potassium Phosphate, pH: 7.4
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2008 Dec 2

R_g^Guinier	2.0	nm
D_max	7.1	nm
Volume^Porod	20	nm³

SASDHE2 – Type 1 insulin-like growth factor receptor ectodomains (IGF-1RΔβ)

Insulin-like growth factor 1 receptor experimental SAS data

Sample:	Insulin-like growth factor 1 receptor dimer, 202 kDa Homo sapiens protein
Buffer:	30 mM Tris, 140 mM NaCl, 0.02% w/v sodium azide,, pH: 7.5
Experiment:	SAXS data collected at Bruker Nanostar, Australian Nuclear Science and Technology Organisation on 2008 Apr 22

Solution structure of ectodomains of the insulin receptor family: the ectodomain of the type 1 insulin-like growth factor receptor displays asymmetry of ligand binding accompanied by limited conformational change. J Mol Biol 394(5):878-92 (2009)
Whitten AE, Smith BJ, Menting JG, Margetts MB, McKern NM, Lovrecz GO, Adams TE, Richards K, Bentley JD, Trewhella J, Ward CW, Lawrence MC

R_g^Guinier	5.1	nm
D_max	16.0	nm
Volume^Porod	357	nm³

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