Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: No model

SASDCK4 – Truncated P5abc subdomain from tetrahymena ribozyme: Static 0.25mM MgCl2

Truncated P5abc subdomain from tetrahymena ribozyme experimental SAS data

Truncated P5abc subdomain from tetrahymena ribozyme Kratky plot

Sample:	Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer:	20mM KCl 0.25mM MgCl2 10mM KMOPS 20uM EDTA, pH: 7
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Jun 17

Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L

R_g^Guinier	2.4	nm
D_max	7.6	nm

SASDCL4 – Truncated P5abc subdomain from tetrahymena ribozyme: Static 0.50mM MgCl2

Sample:	Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer:	0.5mM MgCl2 20mM KCl 10mM KMOPS 20uM EDTA, pH: 7
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Jun 17

Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L

R_g^Guinier	2.3	nm
D_max	7.2	nm

SASDCM4 – Truncated P5abc subdomain from tetrahymena ribozyme: Static 1mM MgCl2

Sample:	Truncated P5abc subdomain from tetrahymena ribozyme monomer, 18 kDa RNA
Buffer:	1mM MgCl2 20mM KCl 10mM KMOPS 20uM EDTA, pH: 7
Experiment:	SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Jun 17

Revealing the distinct folding phases of an RNA three-helix junction. Nucleic Acids Res 46(14):7354-7365 (2018)
Plumridge A, Katz AM, Calvey GD, Elber R, Kirmizialtin S, Pollack L

R_g^Guinier	2.2	nm
D_max	7.2	nm

SASDDC5 – MsbA in stealth nanodisc (SANS, 100% D2O) + 1 mM ADP

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

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, 1 mM ADP, pH: 7.5
Experiment:	SANS data collected at D11, ILL on 2017 Mar 9

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

R_g^Guinier	3.9	nm
D_max	12.5	nm
Volume^Porod	173	nm³

SASDDD5 – MsbA in stealth nanodisc (SAXS)

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

R_g^Guinier	4.8	nm
D_max	16.0	nm
Volume^Porod	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

R_g^Guinier	2.2	nm
D_max	7.3	nm
Volume^Porod	47	nm³

SASDDF5 – NBD-MsbA (+1mM ADP)

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

R_g^Guinier	2.1	nm
D_max	7.3	nm
Volume^Porod	50	nm³

SASDDQ6 – The ferredoxin protease, FusC

Ferredoxin Protease experimental SAS data

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

R_g^Guinier	3.7	nm
D_max	12.8	nm
Volume^Porod	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

R_g^Guinier	3.7	nm
D_max	12.7	nm
Volume^Porod	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

R_g^Guinier	3.7	nm
D_max	13.2	nm
Volume^Porod	156	nm³

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