Small Angle Scattering Biological Data Bank SASBDB

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SASDA84 – RNA Aptamer

Sample:	SRB2m dimer, 33 kDa RNA
Buffer:	Hepes, pH: 7.4
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 24

Characterization of a fluorophore binding RNA aptamer by fluorescence correlation spectroscopy and small angle X-ray scattering. Anal Biochem 389(1):52-62 (2009)
Werner A, Konarev PV, Svergun DI, Hahn U

R_g^Guinier	2.3	nm
D_max	8.0	nm
Volume^Porod	24	nm³

SASDAR5 – ProNGF

Sample:	ProNGF dimer, 45 kDa Mouse submandibulary glands protein
Buffer:	50 mM Naphosphat 0.5 M Ammonium Sulfate(NH4)2SO4, pH: 7
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Oct 25

Intrinsic structural disorder of mouse proNGF. Proteins 75(4):990-1009 (2009)
Paoletti F, Covaceuszach S, Konarev PV, Gonfloni S, Malerba F, Schwarz E, Svergun DI, Cattaneo A, Lamba D

R_g^Guinier	2.6	nm
D_max	8.0	nm
Volume^Porod	92	nm³

SASDLZ6 – Hexamer - monomer equilibrium of Glutamate Synthase

Glutamate synthase [NADPH] large chainGlutamate synthase [NADPH] small chain experimental SAS data

Sample:	Glutamate synthase [NADPH] large chain hexamer, 968 kDa Azospirillum brasilense protein Glutamate synthase [NADPH] small chain hexamer, 296 kDa Azospirillum brasilense protein
Buffer:	25 mM Hepes/KOH, 1 mM EDTA, 1 mM dithiothreitol, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Feb 19

The Subnanometer Resolution Structure of the Glutamate Synthase 1.2-MDa Hexamer by Cryoelectron Microscopy and Its Oligomerization Behavior in Solution Journal of Biological Chemistry 283(13):8237-8249 (2008)
Cottevieille M, Larquet E, Jonic S, Petoukhov M, Caprini G, Paravisi S, Svergun D, Vanoni M, Boisset N

R_g^Guinier	7.7	nm
D_max	22.4	nm

SASDMS4 – Listeria monocytogenes invasion protein internalin B

Sample:	Internalin B monomer, 36 kDa Listeria monocytogenes serotype … protein
Buffer:	25mM Na-phosphate buffer, 150 mM NaCl, 1mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2003 Nov 11

X-ray and Neutron Small-Angle Scattering Analysis of the Complex Formed by the Met Receptor and the Listeria monocytogenes Invasion Protein InlB Journal of Molecular Biology 377(2):489-500 (2008)
Niemann H, Petoukhov M, Härtlein M, Moulin M, Gherardi E, Timmins P, Heinz D, Svergun D

R_g^Guinier	2.8	nm
D_max	9.6	nm
Volume^Porod	54	nm³

SASDLW5 – Cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens

Sample:	Cytochrome c-552 hexamer, 356 kDa Thioalkalivibrio nitratireducens (strain … protein
Buffer:	Tris-borate buffer, pH: 8.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2005 May 8

Isolation and oligomeric composition of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens. Biochemistry (Mosc) 73(2):164-70 (2008)
Tikhonova TV, Slutskaya ES, Filimonenkov AA, Boyko KM, Kleimenov SY, Konarev PV, Polyakov KM, Svergun DI, Trofimov AA, Khomenkov VG, Zvyagilskaya RA, Popov VO

R_g^Guinier

4.8

SASDMB7 – Glucosamine-6-phosphate Synthase from Candida albicans

N-acetylglucosamine kinase 1 experimental SAS data

Sample:	N-acetylglucosamine kinase 1 tetramer, 219 kDa Candida albicans (strain … protein
Buffer:	0.2 M magnesium acetate, 0.1 M sodium cacodylate, pH: 6.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Apr 28

The crystal and solution studies of glucosamine-6-phosphate synthase from Candida albicans. J Mol Biol 372(3):672-88 (2007)
Raczynska J, Olchowy J, Konariev PV, Svergun DI, Milewski S, Rypniewski W

R_g^Guinier	5.1	nm
D_max	16.0	nm
Volume^Porod	421	nm³

SASDHY3 – KinA-Sda complex

Sporulation kinase ASporulation inhibitor sda experimental SAS data

Sample:	Sporulation kinase A dimer, 51 kDa Bacillus subtilis protein Sporulation inhibitor sda dimer, 11 kDa Bacillus subtilis protein
Buffer:	50mM Tris, 200mM NaCl, 150mM Imidazole, pH: 8.5
Experiment:	SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Nov 16

The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. J Mol Biol 368(2):407-20 (2007)
Whitten AE, Jacques DA, Hammouda B, Hanley T, King GF, Guss JM, Trewhella J, Langley DB

R_g^Guinier	2.9	nm
D_max	8.0	nm
Volume^Porod	85	nm³

SASDHZ3 – Sporulation kinase A

Sporulation kinase A experimental SAS data

Sample:	Sporulation kinase A dimer, 51 kDa Bacillus subtilis protein
Buffer:	50mM Tris, 200mM NaCl, 150mM Imidazole, pH: 8.5
Experiment:	SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Mar 18

R_g^Guinier	2.9	nm
D_max	9.5	nm
Volume^Porod	76	nm³

SASDA68 – Aldolase in Tris/HCl

Fructose-bisphosphate aldolase A experimental SAS data

Sample:	Fructose-bisphosphate aldolase A tetramer, 157 kDa Oryctolagus cuniculus protein
Buffer:	100 mM Tris/HCl 100 mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 19

Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering Journal of Applied Crystallography 40(s1):s245-s249 (2007)
Mylonas E, Svergun D

R_g^Guinier	3.6	nm
D_max	10.5	nm

SASDLR7 – The HC Fragment of Tetanus Toxin

Hc fragment of Tetanus toxin experimental SAS data

Sample:	Hc fragment of Tetanus toxin dimer, 103 kDa Clostridium tetani (strain … protein
Buffer:	50 mM sodium phosphate buffer, 300 mM NaCl, pH: 7.8
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2004 May 14

The HC fragment of tetanus toxin forms stable, concentration-dependent dimers via an intermolecular disulphide bond. J Mol Biol 365(1):123-34 (2007)
Qazi O, Bolgiano B, Crane D, Svergun DI, Konarev PV, Yao ZP, Robinson CV, Brown KA, Fairweather N

R_g^Guinier	4.0	nm
D_max	13.2	nm
Volume^Porod	150	nm³

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