Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: Ab initio only

SASDB49 – Single stranded poly-deoxythymidine DNA (30mer, dT30) in 200 mM NaCl

Poly-deoxythymidine (30mer) experimental SAS data

Sample:	Poly-deoxythymidine (30mer) monomer, 9 kDa DNA
Buffer:	1mM Na MOPS, 200mM NaCl, pH: 7
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Apr 1

The impact of base stacking on the conformations and electrostatics of single-stranded DNA. Nucleic Acids Res 45(7):3932-3943 (2017)
Plumridge A, Meisburger SP, Andresen K, Pollack L

R_g^Guinier

2.7

SASDBT6 – GppNHp bound form of full length ObgE from E.coli (ObgE_FL with GppNHp)

Sample:	GTPase ObgE/CgtA monomer, 44 kDa Escherichia coli protein
Buffer:	20 mM Hepes, 300 mM NaCl, 250 mM imidazole, 5 mM MgCl2, 2 mM DTT, 400 µM GppNHp, pH: 7.5
Experiment:	SAXS data collected at SWING, SOLEIL on 2015 Jun 17

Structural and biochemical analysis of Escherichia coli ObgE, a central regulator of bacterial persistence. J Biol Chem 292(14):5871-5883 (2017)
Gkekas S, Singh RK, Shkumatov AV, Messens J, Fauvart M, Verstraeten N, Michiels J, Versées W

R_g^Guinier	3.7	nm
D_max	14.5	nm
Volume^Porod	90	nm³

SASDBV6 – GppNHp bound form of C-terminal deletion mutant of ObgE from E.coli (ObgE_340 with GppNHp)

Sample:	GTPase ObgE/CgtA monomer, 39 kDa Escherichia coli protein
Buffer:	20 mM Hepes, 300 mM NaCl, 250 mM imidazole, 5 mM MgCl2, 2 mM DTT, 400 µM GppNHp, pH: 7.5
Experiment:	SAXS data collected at SWING, SOLEIL on 2015 Mar 12

R_g^Guinier	3.1	nm
D_max	11.4	nm
Volume^Porod	72	nm³

SASDBB9 – GDP bound form of full length ObgE from E.coli (ObgE_FL with GDP)

Sample:	GTPase ObgE/CgtA monomer, 44 kDa Escherichia coli protein
Buffer:	20 mM Hepes, 300 mM NaCl, 250 mM imidazole, 5 mM MgCl2, 2 mM DTT, 400 uM GDP, pH: 7.5
Experiment:	SAXS data collected at SWING, SOLEIL on 2015 Jun 17

R_g^Guinier	3.5	nm
D_max	16.0	nm
Volume^Porod	94673	nm³

SASDBC9 – GDP bound form of C-terminal deletion mutant of ObgE from E.coli (ObgE_340 with GDP)

Sample:	GTPase ObgE/CgtA monomer, 39 kDa Escherichia coli protein
Buffer:	20 mM Hepes, 300 mM NaCl, 250 mM imidazole, 5 mM MgCl2, 2 mM DTT, 400 uM GDP, pH: 7.5
Experiment:	SAXS data collected at Rigaku BioSAXS-2000, on 2015 Feb 1

R_g^Guinier	3.0	nm
D_max	11.0	nm
Volume^Porod	70673	nm³

SASDBD3 – Leishmania braziliensis heat shock protein 90 (Hsp90).

Leishmania braziliensis heat shock protein 90 (Hsp90) experimental SAS data

Sample:	Leishmania braziliensis heat shock protein 90 (Hsp90) dimer, 166 kDa Leishmania braziliensis protein
Buffer:	25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5
Experiment:	SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1

Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering. Int J Biol Macromol 97:503-512 (2017)
Seraphim TV, Silva KP, Dores-Silva PR, Barbosa LR, Borges JC

R_g^Guinier	5.3	nm
D_max	21.0	nm
Volume^Porod	380	nm³

SASDBE3 – Leishmania braziliensis heat shock protein 90 (Hsp90) N domain.

Leishmania braziliensis heat shock protein 90 (Hsp90) N domain experimental SAS data

Sample:	Leishmania braziliensis heat shock protein 90 (Hsp90) N domain monomer, 26 kDa Leishmania braziliensis protein
Buffer:	25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5
Experiment:	SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1

R_g^Guinier	2.0	nm
D_max	7.5	nm
Volume^Porod	40	nm³

SASDBF3 – Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains.

Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains experimental SAS data

Sample:	Leishmania braziliensis heat shock protein 90 (Hsp90) N and M domains monomer, 62 kDa Leishmania braziliensis protein
Buffer:	25 Tris mM 100 mM NaCl 1 mM 2-mercaptoethanol, pH: 7.5
Experiment:	SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2011 Sep 1

R_g^Guinier	3.2	nm
D_max	13.0	nm
Volume^Porod	89	nm³

SASDBU7 – DNA binding domain (DBD) of chromo domain-containing protein 1 (Chd1: 1009-1274)

chromodomain helicase DNA binding domain experimental SAS data

Sample:	Chromodomain helicase DNA binding domain monomer, 31 kDa Saccharomyces cerevisiae protein
Buffer:	50mM Hepes 150mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL X33, DORIS III, DESY on 2009 Nov 20

Structural reorganization of the chromatin remodeling enzyme Chd1 upon engagement with nucleosomes. Elife 6 (2017)
Sundaramoorthy R, Hughes AL, Singh V, Wiechens N, Ryan DP, El-Mkami H, Petoukhov M, Svergun DI, Treutlein B, Quack S, Fischer M, Michaelis J, Böttcher B, Norman DG, Owen-Hughes T

R_g^Guinier	2.6	nm
D_max	8.3	nm

SASDBV7 – Chromo-ATPase-DBD domains of chromo domain-containing protein 1 (Chd1: 133-1305)

Sample:	Chromodomain helicase DNA binding domain monomer, 135 kDa Saccharomyces cerevisiae protein
Buffer:	50mM Hepes 150mM NaCl, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2008 Nov 30

R_g^Guinier	4.2	nm
D_max	15.4	nm
Volume^Porod	280	nm³

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