Small Angle Scattering Biological Data Bank SASBDB

Browse by MACROMOLECULE type: protein

SASDDX6 – The ferredoxin protease, FusC, E83A mutant + 10 µM Arabidopsis ferredoxin

Ferredoxin protease E83A mutantArabidopsis ferredoxin 2 experimental SAS data

Ferredoxin protease E83A mutant Arabidopsis ferredoxin 2 Kratky plot

Sample:	Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer:	20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26

FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants. PLoS Biol 16(8):e2006026 (2018)
Grinter R, Hay ID, Song J, Wang J, Teng D, Dhanesakaran V, Wilksch JJ, Davies MR, Littler D, Beckham SA, Henderson IR, Strugnell RA, Dougan G, Lithgow T

R_g^Guinier	3.7	nm
D_max	13.6	nm
Volume^Porod	149	nm³

SASDDY6 – The ferredoxin protease, FusC, E83A mutant + 20 µM Arabidopsis ferredoxin

Sample:	Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer:	20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26

R_g^Guinier	3.7	nm
D_max	13.6	nm
Volume^Porod	155	nm³

SASDDZ6 – The ferredoxin protease, FusC, E83A mutant + 30 µM Arabidopsis ferredoxin

Sample:	Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer:	20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26

R_g^Guinier	3.7	nm
D_max	14.0	nm
Volume^Porod	156	nm³

SASDD27 – The ferredoxin protease, FusC, E83A mutant + 50 µM Arabidopsis ferredoxin

Sample:	Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer:	20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26

R_g^Guinier	3.8	nm
D_max	14.0	nm
Volume^Porod	160	nm³

SASDD37 – The ferredoxin protease, FusC, E83A mutant + 70 µM Arabidopsis ferredoxin

Sample:	Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer:	20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26

R_g^Guinier	3.7	nm
D_max	14.0	nm
Volume^Porod	165	nm³

SASDD47 – The ferredoxin protease, FusC, E83A mutant + 100 µM Arabidopsis ferredoxin

Sample:	Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer:	20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26

R_g^Guinier	3.7	nm
D_max	13.7	nm
Volume^Porod	177	nm³

SASDD57 – The ferredoxin protease, FusC, E83A mutant + 150 µM Arabidopsis ferredoxin

Sample:	Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer:	20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26

R_g^Guinier	3.8	nm
D_max	14.2	nm
Volume^Porod	178	nm³

SASDD67 – The ferredoxin protease, FusC, E83A mutant + 200 µM Arabidopsis ferredoxin

Sample:	Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer:	20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26

R_g^Guinier	3.7	nm
D_max	14.0	nm
Volume^Porod	175	nm³

SASDD77 – The ferredoxin protease, FusC, E83A mutant + 300 µM Arabidopsis ferredoxin

Sample:	Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer:	20 mM Tris, 150 mM NaCl, pH: 7.8
Experiment:	SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Oct 26

R_g^Guinier	3.7	nm
D_max	14.0	nm
Volume^Porod	180	nm³

SASDDJ9 – Conformation of the R1-3 human dystrophin fragment (SANS)

R1-3 human dystrophin fragment experimental SAS data

Sample:	R1-3 human dystrophin fragment monomer, 39 kDa Homo sapiens protein
Buffer:	20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% D2O, pD 7.5, pH: 7.1
Experiment:	SANS data collected at D22, Institut Laue-Langevin (ILL) on 2016 Nov 7

Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids. Biophys J 115(7):1231-1239 (2018)
Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF

R_g^Guinier	4.2	nm
D_max	17.7	nm
Volume^Porod	46	nm³

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