SASBDB entries for UniProt ID:

SASDCG3 – Nucleolysin TIA-1 isoform p40 (LPATG containing construct for sortase mediated protein ligation)

UniProt ID: P31483-2 (None-None) Nucleolysin TIA-1 isoform p40
Nucleolysin TIA-1 isoform p40 experimental SAS data
Nucleolysin TIA-1 isoform p40 Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 30 kDa Homo sapiens protein
Buffer: 10 mM Potassium Phosphate 50 mM NaCl 10 mM DTT, pH: 6
Experiment: SAXS data collected at Rigaku BioSAXS-1000, SFB 1035, Technische Universität München on 2016 May 4
Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins. Angew Chem Int Ed Engl 56(32):9322-9325 (2017)
Sonntag M, Jagtap PKA, Simon B, Appavou MS, Geerlof A, Stehle R, Gabel F, Hennig J, Sattler M
RgGuinier 2.7 nm
Dmax 10.5 nm
VolumePorod 37 nm3

SASDCH3 – Nucleolysin TIA-1 isoform p40 in complex with U15 RNA (LPATG containing construct for sortase mediated protein ligation)

UniProt ID: (None-None) poly U 15mer

UniProt ID: P31483-2 (None-None) Nucleolysin TIA-1 isoform p40
poly U 15merNucleolysin TIA-1 isoform p40 experimental SAS data
poly U 15mer Nucleolysin TIA-1 isoform p40 Kratky plot
Sample: Poly U 15mer monomer, 5 kDa RNA
Nucleolysin TIA-1 isoform p40 monomer, 30 kDa Homo sapiens protein
Buffer: 10 mM Potassium Phosphate 50 mM NaCl 10 mM DTT, pH: 6
Experiment: SAXS data collected at Rigaku BioSAXS-1000, SFB 1035, Technische Universität München on 2016 May 4
Segmental, Domain-Selective Perdeuteration and Small-Angle Neutron Scattering for Structural Analysis of Multi-Domain Proteins. Angew Chem Int Ed Engl 56(32):9322-9325 (2017)
Sonntag M, Jagtap PKA, Simon B, Appavou MS, Geerlof A, Stehle R, Gabel F, Hennig J, Sattler M
RgGuinier 2.4 nm
Dmax 8.6 nm
VolumePorod 40 nm3

SASDCJ3 – Bovine Serum Albumin

UniProt ID: P02769 (25-607) Serum albumin
Serum albumin experimental SAS data
DAMMIN model
Sample: Serum albumin monomer, 66 kDa Bos taurus protein
Buffer: 25 mM MOPS, 250 mM NaCl, 50 mM KCl, 2 mM TCEP, 0.1% NaN3, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Mar 9
2017 publication guidelines for structural modelling of small-angle scattering data from biomolecules in solution: an update. Acta Crystallogr D Struct Biol 73(Pt 9):710-728 (2017)
Trewhella J, Duff AP, Durand D, Gabel F, Guss JM, Hendrickson WA, Hura GL, Jacques DA, Kirby NM, Kwan AH, Pérez J, Pollack L, Ryan TM, Sali A, Schneidman-Duhovny D, Schwede T, Svergun DI, Sugiyama M, Tainer JA, Vachette P, Westbrook J, Whitten AE
RgGuinier 2.8 nm
Dmax 8.7 nm
VolumePorod 101 nm3

SASDCL3 – Atg1-Atg13 Subcomplex

UniProt ID: Q6CSX2 (562-831) Serine/threonine-protein kinase ATG1

UniProt ID: Q6CWK2 (400-475) Autophagy-related protein 13
Serine/threonine-protein kinase ATG1Autophagy-related protein 13 experimental SAS data
Serine/threonine-protein kinase ATG1 Autophagy-related protein 13 Kratky plot
Sample: Serine/threonine-protein kinase ATG1 dimer, 61 kDa Kluyveromyces lactis protein
Autophagy-related protein 13 dimer, 17 kDa Kluyveromyces lactis protein
Buffer: 20 mM Tris, 200 mM NaCl, 2% glycerol, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2013 Dec 10
Solution structure of the Atg1 complex: implications for the architecture of the phagophore assembly site. Structure 23(5):809-818 (2015)
Köfinger J, Ragusa MJ, Lee IH, Hummer G, Hurley JH
RgGuinier 3.3 nm
Dmax 10.9 nm
VolumePorod 160 nm3

SASDCM3 – Atg17-Atg31-Atg29 Subcomplex

UniProt ID: Q6CS99 (1-423) Autophagy-related protein 17

UniProt ID: Q6CTU8 (1-85) Autophagy-related protein 29

UniProt ID: Q6CX74 (1-143) KLLA0A10637p
Autophagy-related protein 17Autophagy-related protein 29KLLA0A10637p experimental SAS data
Autophagy-related protein 17 Autophagy-related protein 29 KLLA0A10637p Kratky plot
Sample: Autophagy-related protein 17 dimer, 100 kDa Kluyveromyces lactis protein
Autophagy-related protein 29 dimer, 20 kDa Kluyveromyces lactis protein
KLLA0A10637p dimer, 32 kDa Kluyveromyces lactis protein
Buffer: 20 mM Tris, 200 mM NaCl, 2% glycerol, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2013 Dec 10
Solution structure of the Atg1 complex: implications for the architecture of the phagophore assembly site. Structure 23(5):809-818 (2015)
Köfinger J, Ragusa MJ, Lee IH, Hummer G, Hurley JH
RgGuinier 10.1 nm
Dmax 34.0 nm
VolumePorod 848 nm3

SASDCN3 – Phosphoenolpyruvate-protein phosphotransferase

UniProt ID: A0A037YGN3 (1-575) Phosphoenolpyruvate-protein phosphotransferase
Phosphoenolpyruvate-protein phosphotransferase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Phosphoenolpyruvate-protein phosphotransferase dimer, 127 kDa Escherichia coli protein
Buffer: 20mM TRIS buffer, 100 mM NaCl, 10 mM DTT, 4 mM MgCl2, 1 mM EDTA, pH: 7.4
Experiment: SAXS data collected at 12-ID-C, Advanced Photon Source (APS), Argonne National Laboratory on 2010 Aug 23
Solution structure of the 128 kDa enzyme I dimer from Escherichia coli and its 146 kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering. J Am Chem Soc 132(37):13026-45 (2010)
Schwieters CD, Suh JY, Grishaev A, Ghirlando R, Takayama Y, Clore GM
RgGuinier 4.1 nm
Dmax 14.8 nm
VolumePorod 189 nm3

SASDCP3 – Proline utilization A from Bdellovibrio bacteriovorus

UniProt ID: Q6MNK1 (None-None) Bifunctional protein PutA
Bifunctional protein PutA experimental SAS data
DAMMIF model
Sample: Bifunctional protein PutA dimer, 219 kDa Bdellovibrio bacteriovorus protein
Buffer: 50 mM Tris, 125 mM NaCl, 1 mM EDTA, and 1 mM tris(3-hydroxypropyl)phosphine (THP) at pH 7.5,, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Jun 8
Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS J 284(18):3029-3049 (2017)
Korasick DA, Singh H, Pemberton TA, Luo M, Dhatwalia R, Tanner JJ
RgGuinier 4.5 nm
Dmax 14.0 nm
VolumePorod 287 nm3

SASDCQ3 – Proline utilization A from Desulfovibrio vulgaris 1.5 mg/mL

UniProt ID: A0A0E0T6R2 (None-None) Bifunctional protein PutA
Bifunctional protein PutA experimental SAS data
Bifunctional protein PutA Kratky plot
Sample: Bifunctional protein PutA dimer, 229 kDa Desulfovibrio vulgaris protein
Buffer: 50 mM Tris-HCl, 50 mM NaCl, 0.5 mM EDTA, and 0.5 mM THP at pH 7.5., pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2012 Jun 8
Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS J 284(18):3029-3049 (2017)
Korasick DA, Singh H, Pemberton TA, Luo M, Dhatwalia R, Tanner JJ
RgGuinier 4.4 nm
Dmax 16.0 nm
VolumePorod 293 nm3

SASDCR3 – Proline utilization A from Legionella pneumophila 3 mg/mL

UniProt ID: Q5ZUU6 (None-None) Bifunctional protein PutA
Bifunctional protein PutA experimental SAS data
Bifunctional protein PutA Kratky plot
Sample: Bifunctional protein PutA dimer, 238 kDa Legionella pneumophila subsp. … protein
Buffer: 50 mM Tris-HCl, 50 mM NaCl, 0.5 mM EDTA, and 0.5 mM THP at pH 7.5., pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2010 Apr 20
Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS J 284(18):3029-3049 (2017)
Korasick DA, Singh H, Pemberton TA, Luo M, Dhatwalia R, Tanner JJ
RgGuinier 4.6 nm
Dmax 16.0 nm
VolumePorod 291 nm3

SASDCS3 – Proline utilization A from Bradyrhizobium diazoefficiens (formerly Bradyrhizobium japonicum) 2.3 mg/mL

UniProt ID: Q89E26 (None-None) Proline dehydrogenase
Proline dehydrogenase experimental SAS data
Proline dehydrogenase Kratky plot
Sample: Proline dehydrogenase tetramer, 430 kDa Bradyrhizobium diazoefficiens protein
Buffer: 50 mM Tris (pH 7.8), 50 mM NaCl, 0.5 mM Tris(2-carboxyethyl)phosphine, and 5% (v/v) glycerol, pH: 7.8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Dec 16
Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure. FEBS J 284(18):3029-3049 (2017)
Korasick DA, Singh H, Pemberton TA, Luo M, Dhatwalia R, Tanner JJ
RgGuinier 5.3 nm
Dmax 14.1 nm
VolumePorod 541 nm3