Small Angle Scattering Biological Data Bank SASBDB

Browse by ORGANISM: Escherichia coli

SASDEA3 – Labeled thioredoxin (TRX-Alexa488/Alexa594) with denaturant

Thioredoxin 1Alexa Fluor™ 594 C5 MaleimideAlexa Fluor™ 488 C5 Hydroxylamine experimental SAS data

Thioredoxin 1 Alexa Fluor™ 594 C5 Maleimide Alexa Fluor™ 488 C5 Hydroxylamine Kratky plot

Sample:	Thioredoxin 1 monomer, 12 kDa Escherichia coli protein Alexa Fluor™ 594 C5 Maleimide monomer, 1 kDa Alexa Fluor™ 488 C5 Hydroxylamine monomer, 1 kDa
Buffer:	PBS, 10 mM DTT, 6 M urea, 0.3 M KCl, pH: 7.4
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Jun 15

Decoupling of size and shape fluctuations in heteropolymeric sequences reconciles discrepancies in SAXS vs. FRET measurements. Proc Natl Acad Sci U S A 114(31):E6342-E6351 (2017)
Fuertes G, Banterle N, Ruff KM, Chowdhury A, Mercadante D, Koehler C, Kachala M, Estrada Girona G, Milles S, Mishra A, Onck PR, Gräter F, Esteban-Martín S, Pappu RV, Svergun DI, Lemke EA

R_g^Guinier	3.2	nm
D_max	13.9	nm
Volume^Porod	31	nm³

SASDB45 – Trimeric periplasmic holdase chaperone protein Skp

Periplasmic holdase chaperone protein Skp experimental SAS data

Trimeric periplasmic holdase chaperone protein Skp Rg histogram

Sample:	Periplasmic holdase chaperone protein Skp trimer, 47 kDa Escherichia coli protein
Buffer:	25 mM HEPES 150 mM NaCl 1 mM DTT, pH: 7.5
Experiment:	SAXS data collected at EMBL P12, PETRA III on 2013 Sep 24

A Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperone. Structure 25(7):1079-1088.e3 (2017)
Holdbrook DA, Burmann BM, Huber RG, Petoukhov MV, Svergun DI, Hiller S, Bond PJ

R_g^Guinier	3.6	nm
D_max	12.8	nm
Volume^Porod	168	nm³

SASDBS6 – Apo form of full length ObgE from E.coli (ObgE_FL)

Apo form of full length ObgE from E.coli (ObgE_FL) Rg histogram

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, 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	18.1	nm
Volume^Porod	102	nm³

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

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

SASDBU6 – Apo form of the C-terminal deletion mutant of ObgE from E.coli (ObgE_340)

Apo form of the C-terminal deletion mutant of ObgE from E.coli (ObgE_340) Rg histogram

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, pH: 7.5
Experiment:	SAXS data collected at SWING, SOLEIL on 2015 Mar 12

R_g^Guinier	3.1	nm
D_max	11.6	nm
Volume^Porod	70	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

SASDBA9 – E. coli CcdB2-CcdA2-CcdB2 toxin/antitoxin heterohexamer complex

Toxin CcdBAntitoxin CcdAToxin CcdB experimental SAS data

Sample:	Toxin CcdB dimer, 23 kDa Escherichia coli protein Antitoxin CcdA dimer, 17 kDa Escherichia coli protein Toxin CcdB dimer, 23 kDa Escherichia coli protein
Buffer:	10 mM Tris 50 mM NaCl, pH: 7.3
Experiment:	SAXS data collected at SWING, SOLEIL on 2013 Jul 24

Molecular mechanism governing ratio-dependent transcription regulation in the ccdAB operon. Nucleic Acids Res 45(6):2937-2950 (2017)
Vandervelde A, Drobnak I, Hadži S, Sterckx YG, Welte T, De Greve H, Charlier D, Efremov R, Loris R, Lah J

R_g^Guinier	3.4	nm
D_max	12.0	nm
Volume^Porod	92	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

SASDBZ5 – Enzyme I-Ntr (residues 170-424) in complex with NPr (residues 1-85)

Phosphocarrier protein NPrPhosphoenolpyruvate-protein phosphotransferase PtsP experimental SAS data

Sample:	Phosphocarrier protein NPr monomer, 9 kDa Escherichia coli protein Phosphoenolpyruvate-protein phosphotransferase PtsP monomer, 28 kDa Escherichia coli protein
Buffer:	10 mM Tris 150 mM NaCl 0.5 mM EDTA, pH: 7.5
Experiment:	SAXS data collected at Rigaku BioSAXS-1000, NIDDK, NIH on 2015 Jan 30

Structure of the NPr:EIN^Ntr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems. Structure 24(12):2127-2137 (2016)
Strickland M, Stanley AM, Wang G, Botos I, Schwieters CD, Buchanan SK, Peterkofsky A, Tjandra N

R_g^Guinier	2.3	nm
D_max	8.2	nm
Volume^Porod	52	nm³

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