Browse by ORGANISM: other species

SASDD45 – Type II toxin-antitoxin system HicB family antitoxin - HicB protein

Type II toxin-antitoxin system HicB family antitoxin experimental SAS data
PYMOL model
Sample: Type II toxin-antitoxin system HicB family antitoxin tetramer, 63 kDa Burkholderia pseudomallei protein
Buffer: 25 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jul 28
The molecular basis of protein toxin HicA-dependent binding of the protein antitoxin HicB to DNA. J Biol Chem (2018)
Winter AJ, Williams C, Isupov MN, Crocker H, Gromova M, Marsh P, Wilkinson OJ, Dillingham MS, Harmer NJ, Titball RW, Crump MP
RgGuinier 3.0 nm
Dmax 10.5 nm
VolumePorod 112 nm3

SASDD55 – Type II toxin-antitoxin system HicB family antitoxin - HicB protein - bound to addiction module toxin, HicA

Type II toxin-antitoxin system HicB family antitoxinAddiction module toxin, HicA experimental SAS data
PYMOL model
Sample: Type II toxin-antitoxin system HicB family antitoxin tetramer, 63 kDa Burkholderia pseudomallei protein
Addiction module toxin, HicA monomer, 7 kDa Burkholderia pseudomallei protein
Buffer: 25 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2016 Jul 27
The molecular basis of protein toxin HicA-dependent binding of the protein antitoxin HicB to DNA. J Biol Chem (2018)
Winter AJ, Williams C, Isupov MN, Crocker H, Gromova M, Marsh P, Wilkinson OJ, Dillingham MS, Harmer NJ, Titball RW, Crump MP
RgGuinier 3.2 nm
Dmax 11.0 nm
VolumePorod 110 nm3

SASDC75 – Leishmania braziliensis SGT co-chaperone

SGT protein experimental SAS data
DAMFILT model
Sample: SGT protein dimer, 92 kDa Leishmania braziliensis protein
Buffer: 20 mM Potassium Phosphate, 100 mM KCl, 10 mM EDTA, 1 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2014 May 14
Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities. Int J Biol Macromol 118(Pt A):693-706 (2018)
Coto ALS, Seraphim TV, Batista FAH, Dores-Silva PR, Barranco ABF, Teixeira FR, Gava LM, Borges JC
RgGuinier 4.5 nm
Dmax 17.0 nm

SASDDE9 – Synechocystis fluorescence recovery protein FRPcc in the pre-oxidized state (CC mutant)

Fluorescence recovery protein experimental SAS data
CORAL model
Sample: Fluorescence recovery protein dimer, 28 kDa Synechocystis sp. PCC … protein
Buffer: 20 mM Tris, 150 mM NaCl, 3% glycerol, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 1
OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria. Nat Commun 9(1):3869 (2018)
Sluchanko NN, Slonimskiy YB, Shirshin EA, Moldenhauer M, Friedrich T, Maksimov EG
RgGuinier 2.9 nm
Dmax 13.0 nm
VolumePorod 43 nm3

SASDDF9 – Synechocystis orange carotenoid-binding protein devoid of the NTE (OCP-ΔNTE, orange form)

Orange carotenoid-binding protein experimental SAS data
CORAL model
Sample: Orange carotenoid-binding protein monomer, 34 kDa Synechocystis sp. PCC … protein
Buffer: 20 mM Tris, 150 mM NaCl, 3% glycerol, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 1
OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria. Nat Commun 9(1):3869 (2018)
Sluchanko NN, Slonimskiy YB, Shirshin EA, Moldenhauer M, Friedrich T, Maksimov EG
RgGuinier 2.2 nm
Dmax 7.4 nm
VolumePorod 57 nm3

SASDDG9 – The 2:1 complex of Synechocystis disulphide-trapped Fluorescence recovery protein dimer (CC mutant) and orange carotenoid-binding protein-ΔNTE (orange form)

Fluorescence recovery proteinOrange carotenoid-binding protein experimental SAS data
GASBOR model
Sample: Fluorescence recovery protein dimer, 28 kDa Synechocystis sp. PCC … protein
Orange carotenoid-binding protein monomer, 34 kDa Synechocystis sp. PCC … protein
Buffer: 20 mM Tris, 150 mM NaCl, 3% glycerol, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Sep 1
OCP-FRP protein complex topologies suggest a mechanism for controlling high light tolerance in cyanobacteria. Nat Commun 9(1):3869 (2018)
Sluchanko NN, Slonimskiy YB, Shirshin EA, Moldenhauer M, Friedrich T, Maksimov EG
RgGuinier 3.0 nm
Dmax 13.0 nm
VolumePorod 102 nm3

SASDDS8 – Neural/ectodermal development factor IMP-L2

Neural/ectodermal development factor IMP-L2 experimental SAS data
Neural/ectodermal development factor IMP-L2 Kratky plot
Sample: Neural/ectodermal development factor IMP-L2 dimer, 60 kDa Drosophila melanogaster protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at ID14-3, ESRF on 2011 Nov 20
Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones. Nat Commun 9(1):3860 (2018)
Roed NK, Viola CM, Kristensen O, Schluckebier G, Norrman M, Sajid W, Wade JD, Andersen AS, Kristensen C, Ganderton TR, Turkenburg JP, De Meyts P, Brzozowski AM
RgGuinier 3.1 nm
Dmax 12.0 nm
VolumePorod 93 nm3

SASDDT8 – Neural/ectodermal development factor IMP-L2 in complex with insulin-like peptide 5 (DILP5)

Insulin-like peptide 5Neural/ectodermal development factor IMP-L2 experimental SAS data
Insulin-like peptide 5 Neural/ectodermal development factor IMP-L2 Kratky plot
Sample: Insulin-like peptide 5 monomer, 5 kDa Drosophila melanogaster protein
Neural/ectodermal development factor IMP-L2 monomer, 30 kDa Drosophila melanogaster protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at ID14-3, ESRF on 2011 Nov 20
Structures of insect Imp-L2 suggest an alternative strategy for regulating the bioavailability of insulin-like hormones. Nat Commun 9(1):3860 (2018)
Roed NK, Viola CM, Kristensen O, Schluckebier G, Norrman M, Sajid W, Wade JD, Andersen AS, Kristensen C, Ganderton TR, Turkenburg JP, De Meyts P, Brzozowski AM
RgGuinier 2.6 nm
Dmax 9.0 nm
VolumePorod 55 nm3

SASDD95 – Neurexin 1a L5L6

Neurexin 1a L5L6 experimental SAS data
Neurexin 1a L5L6 Rg histogram
Sample: Neurexin 1a L5L6 monomer, 44 kDa protein
Buffer: 20 mM HEPES pH 8, 150 mM NaCl, 0.5mM CaCl2, pH: 8
Experiment: SAXS data collected at Rigaku BioSAXS-1000, Sealy Center For Structural Biology, UTMB-G on 2016 Sep 6
Structural Plasticity of Neurexin 1α: Implications for its Role as Synaptic Organizer. J Mol Biol 430(21):4325-4343 (2018)
Liu J, Misra A, Reddy MVVVS, White MA, Ren G, Rudenko G
RgGuinier 3.0 nm
Dmax 10.0 nm
VolumePorod 69 nm3

SASDDP9 – C-terminal half of pseudorabies virus tegument protein UL37

Tegument protein UL37 experimental SAS data
DAMMIN model
Sample: Tegument protein UL37 monomer, 49 kDa Suid alphaherpesvirus 1 protein
Buffer: 100 mM HEPES 150 mM NaCl 5% glycerol 0.1 mM tris(2-carboxyethyl)phosphine (TCEP), pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2017 Jun 3
The dynamic nature of the conserved tegument protein UL37 of herpesviruses. J Biol Chem 293(41):15827-15839 (2018)
Koenigsberg AL, Heldwein EE
RgGuinier 4.2 nm
Dmax 14.0 nm
VolumePorod 71 nm3