Browse by MODEL: Hybrid

SASDNY2 – Human Anti-TSC Recombinant Antibody (Fab MOR03268) with TSC ligand excess

Fab fragment in complex with small molecule hapten, crystal form-1(1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Fab fragment in complex with small molecule hapten, crystal form-1 monomer, 45 kDa Homo sapiens protein
(1S)-1-AMINO-2-(1H-INDOL-3-YL)ETHANOL monomer, 0 kDa
Buffer: 20 mM Tris–HCl, 50 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Jul 25
Fab MOR03268 Triggers Absorption Shift of a Diagnostic Dye via Packaging in a Solvent-shielded Fab Dimer Interface Journal of Molecular Biology 377(1):206-219 (2008)
Hillig R, Urlinger S, Fanghänel J, Brocks B, Haenel C, Stark Y, Sülzle D, Svergun D, Baesler S, Malawski G, Moosmayer D, Menrad A, Schirner M, Licha K
RgGuinier 3.6 nm
Dmax 15.0 nm
VolumePorod 107 nm3

SASDAN4 – Calmodulin:peptide complex

CalmodulinC-terminal region of human myelin basic protein experimental SAS data
SASREF model
Sample: Calmodulin monomer, 17 kDa Homo sapiens protein
C-terminal region of human myelin basic protein monomer, 2 kDa Homo sapiens protein
Buffer: 25 mM Tris75 200 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Nov 28
Interaction between the C-terminal region of human myelin basic protein and calmodulin: analysis of complex formation and solution structure. BMC Struct Biol 8:10 (2008)
Majava V, Petoukhov MV, Hayashi N, Pirilä P, Svergun DI, Kursula P
RgGuinier 2.1 nm
Dmax 7.0 nm
VolumePorod 36 nm3

SASDLW5 – Cytochrome c nitrite reductase from Thioalkalivibrio nitratireducens

Cytochrome c-552 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Cytochrome c-552 hexamer, 356 kDa Thioalkalivibrio nitratireducens (strain … protein
Buffer: Tris-borate buffer, pH: 8.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 May 8
Isolation and oligomeric composition of cytochrome c nitrite reductase from the haloalkaliphilic bacterium Thioalkalivibrio nitratireducens. Biochemistry (Mosc) 73(2):164-70 (2008)
Tikhonova TV, Slutskaya ES, Filimonenkov AA, Boyko KM, Kleimenov SY, Konarev PV, Polyakov KM, Svergun DI, Trofimov AA, Khomenkov VG, Zvyagilskaya RA, Popov VO
RgGuinier 4.8 nm

SASDAK5 – Myomesin-1 My12-My13

Myomesin-1 experimental SAS data
CRYSOL model
Sample: Myomesin-1 dimer, 46 kDa Homo sapiens protein
Buffer: 25 mM Tris/HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 May 7
Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin. EMBO J 27(1):253-64 (2008)
Pinotsis N, Lange S, Perriard JC, Svergun DI, Wilmanns M
RgGuinier 4.0 nm
Dmax 14.5 nm
VolumePorod 56 nm3

SASDNS2 – Experimental SAXS data for native hemoglobin (Hb) at concentration c = 5 mg/ml

Hemoglobin subunit alphaHemoglobin subunit beta experimental SAS data
GASBOR model
Sample: Hemoglobin subunit alpha monomer, 15 kDa Homo sapiens protein
Hemoglobin subunit beta monomer, 16 kDa Homo sapiens protein
Buffer: Ringer's lactate solution, pH: 6.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Feb 19
Solution Structure of Poly(ethylene) Glycol-Conjugated Hemoglobin Revealed by Small-Angle X-Ray Scattering: Implications for a New Oxygen Therapeutic Biophysical Journal 94(1):173-181 (2008)
Svergun D, Ekström F, Vandegriff K, Malavalli A, Baker D, Nilsson C, Winslow R
RgGuinier 2.4 nm
Dmax 13.0 nm

SASDH43 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN)

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 5 mM EGTA, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.2 nm
Dmax 10.0 nm
VolumePorod 135 nm3

SASDH53 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with calcium

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 10 mM CaCl2, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.4 nm
Dmax 11.0 nm
VolumePorod 160 nm3

SASDH63 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with bound inositol 1,4,5-trisphosphate (IP3)

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 5 mM EGTA, 0.25 mM IP3, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.1 nm
Dmax 8.8 nm
VolumePorod 115 nm3

SASDH73 – N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 (IP3RN) with bound inositol 1,4,5-trisphosphate (IP3) plus calcium

N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 experimental SAS data
BUNCH model
Sample: N-terminal domains of the inositol 1,4,5-trisphosphate receptor type 1 monomer, 70 kDa Mus musculus protein
Buffer: 15 mM Tris, 300 mM NaCl, 1 mM TCEP, 10 mM CaCl2, 0.25 mM IP3, pH: 8
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Apr 12
Ligand-induced conformational changes via flexible linkers in the amino-terminal region of the inositol 1,4,5-trisphosphate receptor. J Mol Biol 373(5):1269-80 (2007)
Chan J, Whitten AE, Jeffries CM, Bosanac I, Mal TK, Ito J, Porumb H, Michikawa T, Mikoshiba K, Trewhella J, Ikura M
RgGuinier 3.2 nm
Dmax 9.6 nm
VolumePorod 132 nm3

SASDL27 – N-Oct-3 POU transcription factor domain in complex with rat CRH DNA

POU domain, class 3, transcription factor 2Rat CRH DNA experimental SAS data
CUSTOM IN-HOUSE model
Sample: POU domain, class 3, transcription factor 2 monomer, 19 kDa Homo sapiens protein
Rat CRH DNA monomer, 15 kDa Rattus norvegicus DNA
Buffer: 50 mM Tris, 0.4 M NaCl, 2% glycerol, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2003 Oct 9
Fine-tuning of intrinsic N-Oct-3 POU domain allostery by regulatory DNA targets Nucleic Acids Research 35(13):4420-4432 (2007)
Alazard R, Mourey L, Ebel C, Konarev P, Petoukhov M, Svergun D, Erard M
RgGuinier 2.9 nm
Dmax 11.0 nm
VolumePorod 41 nm3