SASBDB entries for UniProt ID:

SASDC87 – Deoxyuridine 5'-triphosphate nucleotidohydrolase complex with SaPIbov1 pathogenicity island repressor [3:2] (SEC-SAXS)

UniProt ID: P33316 (94-252) Deoxyuridine 5'-triphosphate nucleotidohydrolase

UniProt ID: E2FZP6 (13-278) SaPIbov1 pathogenicity island repressor
Deoxyuridine 5'-triphosphate nucleotidohydrolaseSaPIbov1 pathogenicity island repressor experimental SAS data
DAMMIF model
Sample: Deoxyuridine 5'-triphosphate nucleotidohydrolase trimer, 54 kDa Homo sapiens protein
SaPIbov1 pathogenicity island repressor dimer, 64 kDa Staphylococcus aureus protein
Buffer: 50 mM HEPES 300 mM NaCl 5 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Jul 10
Structural model of human dUTPase in complex with a novel proteinaceous inhibitor. Sci Rep 8(1):4326 (2018)
Nyíri K, Mertens HDT, Tihanyi B, Nagy GN, Kőhegyi B, Matejka J, Harris MJ, Szabó JE, Papp-Kádár V, Németh-Pongrácz V, Ozohanics O, Vékey K, Svergun DI, Borysik AJ, Vértessy BG
RgGuinier 3.8 nm
Dmax 14.0 nm
VolumePorod 190 nm3

SASDC97 – Ethylene Receptor 1 (DHp + CA + RD domains)

UniProt ID: P49333 (339-738) Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding + receiver domains
Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding + receiver domains experimental SAS data
Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding + receiver domains Kratky plot
Sample: Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding + receiver domains dimer, 88 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM DTT 5 mM ADP, pH: 8.8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 11
Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1). J Biol Chem 290(5):2644-58 (2015)
Mayerhofer H, Panneerselvam S, Kaljunen H, Tuukkanen A, Mertens HD, Mueller-Dieckmann J
RgGuinier 4.0 nm
Dmax 13.9 nm
VolumePorod 144 nm3

SASDCA7 – Ethylene Receptor 1 (DHp + CA domains)

UniProt ID: P49333 (339-589) Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains
Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains experimental SAS data
Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains Kratky plot
Sample: Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains dimer, 55 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris 150 mM NaCl 1 mM DTT 5 mM ADP, pH: 8.8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 11
Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1). J Biol Chem 290(5):2644-58 (2015)
Mayerhofer H, Panneerselvam S, Kaljunen H, Tuukkanen A, Mertens HD, Mueller-Dieckmann J
RgGuinier 2.7 nm
Dmax 8.7 nm
VolumePorod 74 nm3

SASDCB7 – Streptococcus pneumoniae phosphodiesterase Pde2

UniProt ID: A0A0H2ZNP2 (None-None) DHH subfamily 1 protein
DHH subfamily 1 protein experimental SAS data
DHH subfamily 1 protein Kratky plot
Sample: DHH subfamily 1 protein dimer, 70 kDa Streptococcus pneumoniae serotype … protein
Buffer: 20mM Tris, 200 mM NaCl, 5%(v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 23
Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima. Structure 25(12):1887-1897.e4 (2017)
Drexler DJ, Müller M, Rojas-Cordova CA, Bandera AM, Witte G
RgGuinier 2.7 nm
Dmax 7.7 nm
VolumePorod 87 nm3

SASDCC7 – Thermotoga martitima phosphodiesterase TM1595 D80N D154N (inactive mutant)

UniProt ID: Q9X1T1 (None-None) T.maritima PDE
T.maritima PDE experimental SAS data
T.maritima PDE Kratky plot
Sample: T.maritima PDE dimer, 76 kDa Thermotoga maritima protein
Buffer: 25mM Tris 500mM NaCl 3% (v/v) glycerol 2mM MgCl2, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Jun 17
Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima. Structure 25(12):1887-1897.e4 (2017)
Drexler DJ, Müller M, Rojas-Cordova CA, Bandera AM, Witte G
RgGuinier 2.8 nm
Dmax 7.9 nm
VolumePorod 115 nm3

SASDCD7 – Thermotoga maritima phosphodiesterase TM1595 (wildtype, TmPde)

UniProt ID: Q9X1T1 (None-None) Thermotoga maritima phosphodiesterase (wildtype, TmPDE, TM1595)
Thermotoga maritima phosphodiesterase (wildtype, TmPDE, TM1595) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Thermotoga maritima phosphodiesterase (wildtype, TmPDE, TM1595) dimer, 76 kDa Thermotoga maritima protein
Buffer: 20mM Tris, 200 mM NaCl, 5%(v/v) glycerol, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 23
Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima. Structure 25(12):1887-1897.e4 (2017)
Drexler DJ, Müller M, Rojas-Cordova CA, Bandera AM, Witte G
RgGuinier 2.7 nm
Dmax 7.8 nm
VolumePorod 106 nm3

SASDCE7 – Monomeric Sortilin at pH 7.4 in the presence of neurotensin

UniProt ID: Q6PHU5 (None-None) Sortilin, also: Neurotensin-receptor 3
Sortilin, also: Neurotensin-receptor 3 experimental SAS data
Sortilin, also: Neurotensin-receptor 3 Kratky plot
Sample: Sortilin, also: Neurotensin-receptor 3 dimer, 153 kDa Mus musculus protein
Buffer: 25 mM HEPES pH 7.4, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Apr 17
Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release. Nat Commun 8(1):1708 (2017)
Leloup N, Lössl P, Meijer DH, Brennich M, Heck AJR, Thies-Weesie DME, Janssen BJC
RgGuinier 3.3 nm
Dmax 11.7 nm
VolumePorod 192 nm3

SASDCF7 – Dimeric Sortilin at pH 7.4 in the presence of neurotensin

UniProt ID: Q6PHU5 (None-None) Sortilin, also: Neurotensin-receptor 3
Sortilin, also: Neurotensin-receptor 3 experimental SAS data
Sortilin, also: Neurotensin-receptor 3 Kratky plot
Sample: Sortilin, also: Neurotensin-receptor 3 dimer, 153 kDa Mus musculus protein
Buffer: 25 mM HEPES pH 7.4, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Apr 17
Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release. Nat Commun 8(1):1708 (2017)
Leloup N, Lössl P, Meijer DH, Brennich M, Heck AJR, Thies-Weesie DME, Janssen BJC
RgGuinier 3.7 nm
Dmax 13.5 nm
VolumePorod 253 nm3

SASDCG7 – Lys63-linked diubiquitin at pH7.4

UniProt ID: P0CG48 (305-379) Polyubiquitin-C
Polyubiquitin-C experimental SAS data
Polyubiquitin-C Kratky plot
Sample: Polyubiquitin-C dimer, 17 kDa Homo sapiens protein
Buffer: 20mM HEPES, 150mM NaCl, pH: 7.4
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2016 Mar 24
Characterizing Protein Dynamics with Integrative Use of Bulk and Single-Molecule Techniques. Biochemistry 57(3):305-313 (2018)
Liu Z, Gong Z, Cao Y, Ding YH, Dong MQ, Lu YB, Zhang WP, Tang C
RgGuinier 2.0 nm
Dmax 7.0 nm
VolumePorod 22 nm3

SASDCH7 – N-terminal domain of DsbD from N. meningitidis

UniProt ID: Q9JTL9 (23-146) N-terminus of disulfide interchange protein DsbD
N-terminus of disulfide interchange protein DsbD experimental SAS data
DAMMIN model
Sample: N-terminus of disulfide interchange protein DsbD monomer, 14 kDa Neisseria meningitidis protein
Buffer: 25mM HEPES 150mM NaCl, pH: 6.7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2013 May 4
Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis. Acta Crystallogr F Struct Biol Commun 74(Pt 1):31-38 (2018)
Smith RP, Whitten AE, Paxman JJ, Kahler CM, Scanlon MJ, Heras B
RgGuinier 1.8 nm
Dmax 5.7 nm
VolumePorod 17 nm3