Browse by MODEL: No model

SASDD57 – The ferredoxin protease, FusC, E83A mutant + 150 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 3.8 nm
Dmax 14.2 nm
VolumePorod 178 nm3

SASDD67 – The ferredoxin protease, FusC, E83A mutant + 200 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 14.0 nm
VolumePorod 175 nm3

SASDD77 – The ferredoxin protease, FusC, E83A mutant + 300 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 14.0 nm
VolumePorod 180 nm3

SASDDV8 – Boiled chicken egg albumen

Ovalbumin experimental SAS data
Ovalbumin Kratky plot
Sample: Ovalbumin monomer, 43 kDa Gallus gallus protein
Buffer: Water, pH: 7
Experiment: SAXS data collected at Bruker Nonius FR591, University of Pennslyvania on 2013 Jun 27
The Proof Is in the Pidan: Generalizing Proteins as Patchy Particles. ACS Cent Sci 4(7):840-853 (2018)
Cai J, Sweeney AM

SASDDW8 – Chinese century egg albumen (pidan) made from quail egg

Ovalbumin (common quail) experimental SAS data
Ovalbumin (common quail) Kratky plot
Sample: Ovalbumin (common quail) monomer, 42 kDa Coturnix coturnix protein
Buffer: Water, pH: 7
Experiment: SAXS data collected at Bruker Nonius FR591, University of Pennslyvania on 2013 Jun 27
The Proof Is in the Pidan: Generalizing Proteins as Patchy Particles. ACS Cent Sci 4(7):840-853 (2018)
Cai J, Sweeney AM

SASDDX8 – Raw chicken egg albumen

Ovalbumin experimental SAS data
Ovalbumin Kratky plot
Sample: Ovalbumin monomer, 43 kDa Gallus gallus protein
Buffer: Water, pH: 7
Experiment: SAXS data collected at Bruker Nonius FR591, University of Pennslyvania on 2013 Jun 27
The Proof Is in the Pidan: Generalizing Proteins as Patchy Particles. ACS Cent Sci 4(7):840-853 (2018)
Cai J, Sweeney AM

SASDDP6 – Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment (6G08 F(ab))

Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment experimental SAS data
Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment Kratky plot
Sample: Anti-CD32b Antibody Clone 6G08 Antibody Binding Fragment monomer, 46 kDa Homo sapiens protein
Buffer: 50mM HEPES, 150mM KCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Dec 5
Evaluating Anti-CD32b F(ab) Conformation Using Molecular Dynamics and Small-Angle X-Ray Scattering. Biophys J 115(2):289-299 (2018)
Sutton EJ, Bradshaw RT, Orr CM, Frendéus B, Larsson G, Teige I, Cragg MS, Tews I, Essex JW
RgGuinier 2.6 nm
Dmax 7.3 nm
VolumePorod 68 nm3

SASDDB6 – Small glutamine-rich tetratricopeptide repeat-containing protein alpha (full length; SGTA_FL)

Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length experimental SAS data
Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length Kratky plot
Sample: Small glutamine-rich tetratricopeptide repeat-containing protein alpha full length dimer, 68 kDa Homo sapiens protein
Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 5
Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control. BMC Biol 16(1):76 (2018)
Martínez-Lumbreras S, Krysztofinska EM, Thapaliya A, Spilotros A, Matak-Vinkovic D, Salvadori E, Roboti P, Nyathi Y, Muench JH, Roessler MM, Svergun DI, High S, Isaacson RL
RgGuinier 4.2 nm

SASDDC6 – Small glutamine-rich tetratricopeptide repeat-containing protein alpha (N-terminal-TPR domains; SGTA_NT)

Small glutamine-rich tetratricopeptide repeat-containing protein alpha Nterminal-TPR domains experimental SAS data
Small glutamine-rich tetratricopeptide repeat-containing protein alpha Nterminal-TPR domains Kratky plot
Sample: Small glutamine-rich tetratricopeptide repeat-containing protein alpha Nterminal-TPR domains dimer, 47 kDa Homo sapiens protein
Buffer: 10 mM potassium phosphate, 100 mM NaCl, pH: 6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 5
Structural complexity of the co-chaperone SGTA: a conserved C-terminal region is implicated in dimerization and substrate quality control. BMC Biol 16(1):76 (2018)
Martínez-Lumbreras S, Krysztofinska EM, Thapaliya A, Spilotros A, Matak-Vinkovic D, Salvadori E, Roboti P, Nyathi Y, Muench JH, Roessler MM, Svergun DI, High S, Isaacson RL
RgGuinier 3.6 nm

SASDDV5 – 4-hydroxy-tetrahydrodipicolinate synthase (DHDPS-apo) from C. botulinum

4-hydroxy-tetrahydrodipicolinate synthase from Clostridium botulinum experimental SAS data
4-hydroxy-tetrahydrodipicolinate synthase from Clostridium botulinum Kratky plot
Sample: 4-hydroxy-tetrahydrodipicolinate synthase from Clostridium botulinum tetramer, 126 kDa Clostridium botulinum protein
Buffer: 20mM Tris, 150mM NaCl, pH: 8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2010 Nov 26
Substrate Locking Promotes Dimer-Dimer Docking of an Enzyme Antibiotic Target. Structure 26(7):948-959.e5 (2018)
Atkinson SC, Dogovski C, Wood K, Griffin MDW, Gorman MA, Hor L, Reboul CF, Buckle AM, Wuttke J, Parker MW, Dobson RCJ, Perugini MA
RgGuinier 3.2 nm
Dmax 9.0 nm
VolumePorod 159 nm3