SASBDB entries for UniProt ID:

SASDC54 – Envelope of Col H PKD-PKD-CBD complexed with mini-collagen

UniProt ID: Q46085 (717-1021) ColH protein

UniProt ID: (None-None) Collagenous Peptide model [(PPG)10]
ColH proteinCollagenous Peptide model [(PPG)10] experimental SAS data
DAMMIF model
Sample: ColH protein monomer, 34 kDa Hathewaya histolytica protein
Collagenous Peptide model [(PPG)10] trimer, 10 kDa synthetic construct protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Oct 12
Ca2+ -induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation. FEBS J 285(17):3254-3269 (2018)
Caviness P, Bauer R, Tanaka K, Janowska K, Roeser JR, Harter D, Sanders J, Ruth C, Matsushita O, Sakon J
RgGuinier 3.3 nm
Dmax 14.2 nm
VolumePorod 38 nm3

SASDC64 – Envelope of Col G PKD-CBD-CBD complexed with mini-collagen

UniProt ID: (None-None) Collagenous Peptide model [(PPG)10]

UniProt ID: Q9X721 (786-1118) ColG Collagenase
Collagenous Peptide model [(PPG)10]ColG Collagenase experimental SAS data
DAMMIF model
Sample: Collagenous Peptide model [(PPG)10] trimer, 9 kDa synthetic construct protein
ColG Collagenase monomer, 37 kDa Hathewaya histolytica protein
Buffer: 50 mM HEPES, 100 mM NaCl, 5 mM CaCl2, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Oct 12
Ca2+ -induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation. FEBS J 285(17):3254-3269 (2018)
Caviness P, Bauer R, Tanaka K, Janowska K, Roeser JR, Harter D, Sanders J, Ruth C, Matsushita O, Sakon J
RgGuinier 4.1 nm
Dmax 19.3 nm
VolumePorod 70 nm3

SASDCW4 – Bovine β Cardiac Myosin S1 fragment (Myosin-7) MgADP.VO4+OM

UniProt ID: Q9BE39 (None-None) Bovine β Cardiac Myosin S1 fragment
Bovine β Cardiac Myosin S1 fragment experimental SAS data
Bovine β Cardiac Myosin S1 fragment Kratky plot
Sample: Bovine β Cardiac Myosin S1 fragment monomer, 117 kDa Bos taurus protein
Buffer: 10 mM HEPES, 50 mM NaCl, 1 mM NaN3, 2.5 mM MgCl2, 2 mM ADP, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Mar 1
Mechanistic and structural basis for activation of cardiac myosin force production by omecamtiv mecarbil. Nat Commun 8(1):190 (2017)
Planelles-Herrero VJ, Hartman JJ, Robert-Paganin J, Malik FI, Houdusse A
RgGuinier 3.6 nm
Dmax 12.6 nm
VolumePorod 162 nm3

SASDCX4 – Bovine β Cardiac Myosin S1 fragment (Myosin-7) MgADP+OM

UniProt ID: Q9BE39 (None-None) Bovine β Cardiac Myosin S1 fragment
Bovine β Cardiac Myosin S1 fragment experimental SAS data
Bovine β Cardiac Myosin S1 fragment Kratky plot
Sample: Bovine β Cardiac Myosin S1 fragment monomer, 117 kDa Bos taurus protein
Buffer: 10 mM HEPES, 50 mM NaCl, 1 mM NaN3, 2.5 mM MgCl2, 2 mM ADP, 1 mM TCEP, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Mar 1
Mechanistic and structural basis for activation of cardiac myosin force production by omecamtiv mecarbil. Nat Commun 8(1):190 (2017)
Planelles-Herrero VJ, Hartman JJ, Robert-Paganin J, Malik FI, Houdusse A
RgGuinier 4.0 nm
Dmax 11.5 nm
VolumePorod 161 nm3

SASDCY4 – RNase E 603-850

UniProt ID: Q46977 (603-850) RNase E 603-850
RNase E 603-850 experimental SAS data
RNase E 603-850 Rg histogram
Sample: RNase E 603-850 monomer, 30 kDa Escherichia coli protein
Buffer: 50 mM Tris HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v), pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Dec 5
Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. Nucleic Acids Res 46(1):387-402 (2018)
Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF
RgGuinier 5.3 nm
Dmax 27.5 nm
VolumePorod 139 nm3

SASDCZ4 – RNase E 603-850/ATP-dependent RNA helicase (RhlB) binary complex

UniProt ID: Q46977 (603-850) RNase E 603-850

UniProt ID: W8ZZD4 (1-421) ATP-dependent RNA helicase RhlB
RNase E 603-850ATP-dependent RNA helicase RhlB experimental SAS data
GASBOR model
Sample: RNase E 603-850 monomer, 30 kDa Escherichia coli protein
ATP-dependent RNA helicase RhlB monomer, 47 kDa Escherichia coli protein
Buffer: 50 mM Tris HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v), pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2016 Feb 11
Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. Nucleic Acids Res 46(1):387-402 (2018)
Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF
RgGuinier 5.4 nm
Dmax 29.5 nm
VolumePorod 183 nm3

SASDC25 – RNase E 603-850/ATP-dependent RNA helicase (RhlB)/enolase ternary complex

UniProt ID: Q46977 (603-850) RNase E 603-850

UniProt ID: W8ZZD4 (1-421) ATP-dependent RNA helicase RhlB

UniProt ID: A1AEW7 (1-432) Enolase
RNase E 603-850ATP-dependent RNA helicase RhlBEnolase experimental SAS data
GASBOR model
Sample: RNase E 603-850 monomer, 30 kDa Escherichia coli protein
ATP-dependent RNA helicase RhlB monomer, 47 kDa Escherichia coli protein
Enolase dimer, 91 kDa Escherichia coli protein
Buffer: 50 mM Tris HCl, 100 mM NaCl, 100 mM KCl, 10 mM MgCl2, 10 mM DTT and 5 % glycerol (v/v), pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2014 Jul 16
Analysis of the natively unstructured RNA/protein-recognition core in the Escherichia coli RNA degradosome and its interactions with regulatory RNA/Hfq complexes. Nucleic Acids Res 46(1):387-402 (2018)
Bruce HA, Du D, Matak-Vinkovic D, Bandyra KJ, Broadhurst RW, Martin E, Sobott F, Shkumatov AV, Luisi BF
RgGuinier 6.4 nm
Dmax 30.5 nm
VolumePorod 280 nm3

SASDC45 – Alpha domain of autotransporter protein UpaB from UPEC

UniProt ID: A0A0H2V5A3 (37-500) Alpha domain of autotransporter protein UpaB
Alpha domain of autotransporter protein UpaB experimental SAS data
CORAL model
Sample: Alpha domain of autotransporter protein UpaB monomer, 48 kDa E. Coli CFT073 protein
Buffer: 25 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 May 1
Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules. Nat Commun 10(1):1967 (2019)
Paxman JJ, Lo AW, Sullivan MJ, Panjikar S, Kuiper M, Whitten AE, Wang G, Luan CH, Moriel DG, Tan L, Peters KM, Phan MD, Gee CL, Ulett GC, Schembri MA, Heras B
RgGuinier 2.9 nm
Dmax 10.5 nm
VolumePorod 66 nm3

SASDC55 – Plasmodium falciparum p23A

UniProt ID: Q8I2N9 (None-None) CS domain protein, putative
CS domain protein, putative experimental SAS data
DAMFILT model
Sample: CS domain protein, putative monomer, 19 kDa Plasmodium falciparum protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 2 mM EDTA, 1 mM B-mercaptoethanol, pH: 7.4
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2015 May 26
Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome. Int J Biol Macromol 108:193-204 (2018)
Silva NSM, Seraphim TV, Minari K, Barbosa LRS, Borges JC
RgGuinier 2.5 nm
Dmax 8.5 nm

SASDC65 – Plasmodium falciparum p23B

UniProt ID: Q8IKU1 (None-None) Co-chaperone p23
Co-chaperone p23 experimental SAS data
DAMFILT model
Sample: Co-chaperone p23 monomer, 31 kDa Plasmodium falciparum protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 2 mM EDTA, 1 mM B-mercaptoethanol, pH: 7.4
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2015 May 26
Comparative studies of the low-resolution structure of two p23 co-chaperones for Hsp90 identified in Plasmodium falciparum genome. Int J Biol Macromol 108:193-204 (2018)
Silva NSM, Seraphim TV, Minari K, Barbosa LRS, Borges JC
RgGuinier 3.7 nm
Dmax 13.0 nm