Browse by MACROMOLECULE type: protein

SASDMB7 – Glucosamine-6-phosphate Synthase from Candida albicans

N-acetylglucosamine kinase 1 experimental SAS data
DAMMIN model
Sample: N-acetylglucosamine kinase 1 tetramer, 219 kDa Candida albicans (strain … protein
Buffer: 0.2 M magnesium acetate, 0.1 M sodium cacodylate, pH: 6.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Apr 28
The crystal and solution studies of glucosamine-6-phosphate synthase from Candida albicans. J Mol Biol 372(3):672-88 (2007)
Raczynska J, Olchowy J, Konariev PV, Svergun DI, Milewski S, Rypniewski W
RgGuinier 5.1 nm
Dmax 16.0 nm
VolumePorod 421 nm3

SASDAC4 – FilaminC 23-24

Filamin C 23-24 experimental SAS data
DAMMIN model
Sample: Filamin C 23-24 dimer, 40 kDa Escherichia coli protein
Buffer: 20 mM Tris-HCl 50 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Jun 17
Crystal structure of human filamin C domain 23 and small angle scattering model for filamin C 23-24 dimer. J Mol Biol 368(4):1011-23 (2007)
Sjekloća L, Pudas R, Sjöblom B, Konarev P, Carugo O, Rybin V, Kiema TR, Svergun D, Ylänne J, Djinović Carugo K
RgGuinier 3.5 nm
Dmax 13.0 nm
VolumePorod 75 nm3

SASDHY3 – KinA-Sda complex

Sporulation kinase ASporulation inhibitor sda experimental SAS data
SASREF model
Sample: Sporulation kinase A dimer, 51 kDa Bacillus subtilis protein
Sporulation inhibitor sda dimer, 11 kDa Bacillus subtilis protein
Buffer: 50mM Tris, 200mM NaCl, 150mM Imidazole, pH: 8.5
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Nov 16
The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. J Mol Biol 368(2):407-20 (2007)
Whitten AE, Jacques DA, Hammouda B, Hanley T, King GF, Guss JM, Trewhella J, Langley DB
RgGuinier 2.9 nm
Dmax 8.0 nm
VolumePorod 85 nm3

SASDHZ3 – Sporulation kinase A

Sporulation kinase A experimental SAS data
SASREF model
Sample: Sporulation kinase A dimer, 51 kDa Bacillus subtilis protein
Buffer: 50mM Tris, 200mM NaCl, 150mM Imidazole, pH: 8.5
Experiment: SAXS data collected at Bruker Nanostar II, Australian Nuclear Science and Technology Organisation/Australian Centre for Neutron Scattering on 2006 Mar 18
The structure of the KinA-Sda complex suggests an allosteric mechanism of histidine kinase inhibition. J Mol Biol 368(2):407-20 (2007)
Whitten AE, Jacques DA, Hammouda B, Hanley T, King GF, Guss JM, Trewhella J, Langley DB
RgGuinier 2.9 nm
Dmax 9.5 nm
VolumePorod 76 nm3

SASDA68 – Aldolase in Tris/HCl

Fructose-bisphosphate aldolase A experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Fructose-bisphosphate aldolase A tetramer, 157 kDa Oryctolagus cuniculus protein
Buffer: 100 mM Tris/HCl 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 19
Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering Journal of Applied Crystallography 40(s1):s245-s249 (2007)
Mylonas E, Svergun D
RgGuinier 3.6 nm
Dmax 10.5 nm

SASDA78 – Carbonic Anhydrase in Tris/HCl

Carbonic anhydrase 2 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Carbonic anhydrase 2 monomer, 29 kDa Bos taurus protein
Buffer: 100 mM Tris/HCl 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 19
Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering Journal of Applied Crystallography 40(s1):s245-s249 (2007)
Mylonas E, Svergun D
RgGuinier 2.1 nm
Dmax 6.0 nm

SASDA98 – Thyroglobulin in Tris/HCl

Thyroglobulin experimental SAS data
DAMMIN model
Sample: Thyroglobulin dimer, 606 kDa Bos taurus protein
Buffer: 100 mM Tris/HCl 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 19
Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering Journal of Applied Crystallography 40(s1):s245-s249 (2007)
Mylonas E, Svergun D
RgGuinier 7.9 nm
Dmax 24.0 nm

SASDAA8 – Chymotrypsinogen A in Tris/HCl

Chymotrypsinogen A experimental SAS data
CRYSOL model
Sample: Chymotrypsinogen A monomer, 26 kDa Bos taurus protein
Buffer: 100 mM Tris/HCl 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 19
Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering Journal of Applied Crystallography 40(s1):s245-s249 (2007)
Mylonas E, Svergun D
RgGuinier 1.9 nm
Dmax 5.0 nm

SASDMA7 – Prion protein aggregate in solution

Major prion protein experimental SAS data
DAMMIN model
Sample: Major prion protein 24-mer, 664 kDa Homo sapiens protein
Buffer: 5 mM sodium acetate, pH: 5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2005 Jun 2
Structural characterization of beta-sheeted oligomers formed on the pathway of oxidative prion protein aggregation in vitro. J Struct Biol 157(2):308-20 (2007)
Redecke L, von Bergen M, Clos J, Konarev PV, Svergun DI, Fittschen UE, Broekaert JA, Bruns O, Georgieva D, Mandelkow E, Genov N, Betzel C
RgGuinier 9.8 nm
Dmax 32.0 nm
VolumePorod 3320 nm3

SASDNB2 – Human NK inhibitory receptor IRp60 with an immunoglobulin-like fold

CMRF35-like molecule 8 experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: CMRF35-like molecule 8 monomer, 12 kDa Homo sapiens protein
Buffer: MES buffer with 3mM DTT, pH: 5.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 Apr 6
Molecular analysis and solution structure from small-angle X-ray scattering of the human natural killer inhibitory receptor IRp60 (CD300a) International Journal of Biological Macromolecules 40(3):193-200 (2007)
Dimasi N, Roessle M, Moran O, Candiano G, Svergun D, Biassoni R
RgGuinier 2.0 nm
Dmax 7.0 nm
VolumePorod 22 nm3