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

SASDNN2 – Experimental SAXS data for hemoglobin conjucted with six-seven copies of PEG dimer (Hb2) at concentration c = 21 mg/ml

Human hemoglobin conjugated with six-seven copies of 5-kDa PEG experimental SAS data
Human hemoglobin conjugated with six-seven copies of 5-kDa PEG Kratky plot
Sample: Human hemoglobin conjugated with six-seven copies of 5-kDa PEG dimer, 62 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 3.0 nm

SASDNP2 – Experimental SAXS data for hemoglobin conjucted with six-seven copies of PEG dimer (Hb5)

Human hemoglobin conjugated with six-seven copies of 5-kDa PEG experimental SAS data
GASBOR model
Sample: Human hemoglobin conjugated with six-seven copies of 5-kDa PEG dimer, 62 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 3.3 nm
Dmax 13.0 nm

SASDNQ2 – Experimental SAXS data for hemoglobin conjucted with two copies of PEG dimer (Hb2) at concentration c = 25 mg/ml

Human hemoglobin conjugated with two copies of 5-kDa PEG experimental SAS data
Human hemoglobin conjugated with two copies of 5-kDa PEG Kratky plot
Sample: Human hemoglobin conjugated with two copies of 5-kDa PEG dimer, 62 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

SASDNR2 – Experimental SAXS data for hemoglobin conjucted with two copies of PEG dimer (Hb2)

Human hemoglobin conjugated with two copies of 5-kDa PEG experimental SAS data
GASBOR model
Sample: Human hemoglobin conjugated with two copies of 5-kDa PEG dimer, 62 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 2.8 nm
Dmax 13.0 nm

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

SASDNT2 – Experimental SAXS data for native hemoglobin (Hb) at concentration c = 31.25 mg/ml

Hemoglobin subunit alphaHemoglobin subunit beta experimental SAS data
Hemoglobin subunit alpha Hemoglobin subunit beta Kratky plot
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 2.2 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

4338 hits found.