Browse by MACROMOLECULE type: protein

SASDDD5 – MsbA in stealth nanodisc (SAXS)

Lipid A export ATP-binding/permease protein MsbAMembrane scaffold protein 1D1 (deuterated, 75%)1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) experimental SAS data
Lipid A export ATP-binding/permease protein MsbA Membrane scaffold protein 1D1 (deuterated, 75%) 1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl) Kratky plot
Sample: Lipid A export ATP-binding/permease protein MsbA dimer, 133 kDa Escherichia coli protein
Membrane scaffold protein 1D1 (deuterated, 75%) dimer, 49 kDa protein
1-palmitoyl-2-palmitoleoyl-sn-glycero-3-phosphocholine (deuteration: 78% head, 92% acyl), 1 kDa Escherichia coli
Buffer: 30 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 8
Conformational States of ABC Transporter MsbA in a Lipid Environment Investigated by Small-Angle Scattering Using Stealth Carrier Nanodiscs. Structure 26(8):1072-1079.e4 (2018)
Josts I, Nitsche J, Maric S, Mertens HD, Moulin M, Haertlein M, Prevost S, Svergun DI, Busch S, Forsyth VT, Tidow H
RgGuinier 4.8 nm
Dmax 16.0 nm
VolumePorod 607 nm3

SASDDE5 – NBD-MsbA (apo)

Nucleotide Binding Domain of Lipid A export ATP-binding/permease protein MsbA experimental SAS data
Nucleotide Binding Domain of Lipid A export ATP-binding/permease protein MsbA Kratky plot
Sample: Nucleotide Binding Domain of Lipid A export ATP-binding/permease protein MsbA monomer, 27 kDa Escherichia coli protein
Buffer: 30 mM Tris, 150 mM NaCl, 0.5 mM TCEP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 May 30
Conformational States of ABC Transporter MsbA in a Lipid Environment Investigated by Small-Angle Scattering Using Stealth Carrier Nanodiscs. Structure 26(8):1072-1079.e4 (2018)
Josts I, Nitsche J, Maric S, Mertens HD, Moulin M, Haertlein M, Prevost S, Svergun DI, Busch S, Forsyth VT, Tidow H
RgGuinier 2.2 nm
Dmax 7.3 nm
VolumePorod 47 nm3

SASDDF5 – NBD-MsbA (+1mM ADP)

Nucleotide Binding Domain of Lipid A export ATP-binding/permease protein MsbA experimental SAS data
Nucleotide Binding Domain of Lipid A export ATP-binding/permease protein MsbA Kratky plot
Sample: Nucleotide Binding Domain of Lipid A export ATP-binding/permease protein MsbA monomer, 27 kDa Escherichia coli protein
Buffer: 30 mM Tris, 150 mM NaCl, 0.5 mM TCEP, 1 mM ADP, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 May 30
Conformational States of ABC Transporter MsbA in a Lipid Environment Investigated by Small-Angle Scattering Using Stealth Carrier Nanodiscs. Structure 26(8):1072-1079.e4 (2018)
Josts I, Nitsche J, Maric S, Mertens HD, Moulin M, Haertlein M, Prevost S, Svergun DI, Busch S, Forsyth VT, Tidow H
RgGuinier 2.1 nm
Dmax 7.3 nm
VolumePorod 50 nm3

SASDDQ6 – The ferredoxin protease, FusC

Ferredoxin Protease experimental SAS data
Ferredoxin Protease Kratky plot
Sample: Ferredoxin Protease monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.03 % NaN3, 5.0 % glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 6
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
RgGuinier 3.7 nm
Dmax 12.8 nm
VolumePorod 152 nm3

SASDDR6 – The ferredoxin protease, FusC, E83A mutant

Ferredoxin protease E83A mutant experimental SAS data
Ferredoxin protease E83A mutant Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Buffer: 20 mM Tris HCl, 150 nM NaCl, 0.02 % NaN3, 5% glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 6
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
RgGuinier 3.7 nm
Dmax 12.7 nm
VolumePorod 152 nm3

SASDDS6 – The ferredoxin protease, FusC, with Arabidopsis ferredoxin (co-SEC-SAXS)

Ferredoxin ProteaseArabidopsis ferredoxin 2 experimental SAS data
Ferredoxin Protease Arabidopsis ferredoxin 2 Kratky plot
Sample: Ferredoxin Protease monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 protein
Arabidopsis ferredoxin 2 monomer, 11 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris HCl, 150 nM NaCl, 0.02 % NaN3, 5% glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 6
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
RgGuinier 3.7 nm
Dmax 13.2 nm
VolumePorod 156 nm3

SASDDT6 – The ferredoxin protease, FusC, E83A mutant with Arabidopsis ferredoxin (co-SEC-SAXS)

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 HCl, 150 nM NaCl, 0.02 % NaN3, 5% glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 6
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
RgGuinier 3.6 nm
Dmax 12.7 nm
VolumePorod 161 nm3

SASDDU6 – The ferredoxin protease, FusC, E83A mutant

Ferredoxin protease E83A mutant experimental SAS data
Ferredoxin protease E83A mutant Kratky plot
Sample: Ferredoxin protease E83A mutant monomer, 101 kDa Pectobacterium atrosepticum SCRI1043 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
RgGuinier 3.7 nm
Dmax 13.8 nm
VolumePorod 152 nm3

SASDDV6 – The ferredoxin protease, FusC, E83A mutant + 3 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
RgGuinier 3.7 nm
Dmax 13.8 nm
VolumePorod 150 nm3

SASDDW6 – The ferredoxin protease, FusC, E83A mutant + 5 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
RgGuinier 3.7 nm
Dmax 13.7 nm
VolumePorod 148 nm3