Browse by MACROMOLECULE type: protein

SASDAA6 – Human serum albumin monomer and mixtures

Human serum albumin monomer experimental SAS data
DAMMIF model
Sample: Human serum albumin monomer monomer, 66 kDa Homo sapiens protein
Buffer: 50 mM HEPES, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 22
Correlation Map, a goodness-of-fit test for one-dimensional X-ray scattering spectra. Nat Methods 12(5):419-22 (2015)
Franke D, Jeffries CM, Svergun DI
RgGuinier 2.8 nm
Dmax 8.4 nm
VolumePorod 103 nm3

SASDAB6 – Xylose Isomerase

Xylose Isomerase experimental SAS data
DAMMIF model
Sample: Xylose Isomerase tetramer, 173 kDa Streptomyces rubiginosus protein
Buffer: 20 mM HEPES 200 mM Na2SO4 50 mM K2SO4 500 % v/v D2O 1 mM MgCl2, pH: 6.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Dec 10
Correlation Map, a goodness-of-fit test for one-dimensional X-ray scattering spectra. Nat Methods 12(5):419-22 (2015)
Franke D, Jeffries CM, Svergun DI
RgGuinier 3.2 nm
Dmax 9.1 nm
VolumePorod 234 nm3

SASDAL6 – Wild-type chalcone isomerase, ligand-free

Bacterial chalcone isomerase experimental SAS data
Bacterial chalcone isomerase Kratky plot
Sample: Bacterial chalcone isomerase hexamer, 194 kDa Eubacterium ramulus protein
Buffer: 50 mM sodium phosphate, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 23
Structure and catalytic mechanism of the evolutionarily unique bacterial chalcone isomerase. Acta Crystallogr D Biol Crystallogr 71(Pt 4):907-17 (2015)
Thomsen M, Tuukkanen A, Dickerhoff J, Palm GJ, Kratzat H, Svergun DI, Weisz K, Bornscheuer UT, Hinrichs W
RgGuinier 4.0 nm
Dmax 13.0 nm
VolumePorod 320 nm3

SASDAM6 – Naringenin-bound chalcone isomerase

Chalcone isomerase with Naringenin experimental SAS data
Chalcone isomerase with Naringenin Kratky plot
Sample: Chalcone isomerase with Naringenin hexamer, 194 kDa Eubacterium ramulus protein
Buffer: 50 mM sodium phosphate, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 23
Structure and catalytic mechanism of the evolutionarily unique bacterial chalcone isomerase. Acta Crystallogr D Biol Crystallogr 71(Pt 4):907-17 (2015)
Thomsen M, Tuukkanen A, Dickerhoff J, Palm GJ, Kratzat H, Svergun DI, Weisz K, Bornscheuer UT, Hinrichs W
RgGuinier 3.7 nm
Dmax 11.0 nm
VolumePorod 320 nm3

SASDAN6 – Chalcone isomerase, CHI_Δlid construct

Chalcone isomerase deltaLid experimental SAS data
Chalcone isomerase deltaLid Kratky plot
Sample: Chalcone isomerase deltaLid hexamer, 181 kDa Eubacterium ramulus protein
Buffer: 50 mM sodium phosphate, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 23
Structure and catalytic mechanism of the evolutionarily unique bacterial chalcone isomerase. Acta Crystallogr D Biol Crystallogr 71(Pt 4):907-17 (2015)
Thomsen M, Tuukkanen A, Dickerhoff J, Palm GJ, Kratzat H, Svergun DI, Weisz K, Bornscheuer UT, Hinrichs W
RgGuinier 3.6 nm
Dmax 11.0 nm
VolumePorod 270 nm3

SASDAT6 – Integrin beta4, fragment of the cytoplasmic region encompassing the third and fourth FnIII domains

Integrin beta-4 experimental SAS data
DAMMIF model
Sample: Integrin beta-4 monomer, 23 kDa Homo sapiens protein
Buffer: 20 mM Sodium Phosphate 150 mM NaCl 5% glycerol 3 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Aug 6
Combination of X-ray crystallography, SAXS and DEER to obtain the structure of the FnIII-3,4 domains of integrin α6β4. Acta Crystallogr D Biol Crystallogr 71(Pt 4):969-85 (2015)
Alonso-García N, García-Rubio I, Manso JA, Buey RM, Urien H, Sonnenberg A, Jeschke G, de Pereda JM
RgGuinier 2.2 nm
Dmax 7.0 nm
VolumePorod 32 nm3

SASDAA7 – Heterotetramer of histidine protein kinase and response regulator

Histidine protein kinaseResponse regulator experimental SAS data
BUNCH model
Sample: Histidine protein kinase dimer, 54 kDa Streptococcus pneumoniae protein
Response regulator dimer, 61 kDa Streptococcus pneumoniae protein
Buffer: 20 mM Tris 200 mM NaCl 5% (v/v) Glycerol 5 mM β-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at Bruker Nanostar, IBBMC on 2012 May 16
Modeling the ComD/ComE/comcde interaction network using small angle X-ray scattering. FEBS J 282(8):1538-53 (2015)
Sanchez D, Boudes M, van Tilbeurgh H, Durand D, Quevillon-Cheruel S
RgGuinier 4.0 nm
Dmax 16.0 nm
VolumePorod 175 nm3

SASDBL2 – MBP-PICK1 fusion

Maltose Binding Protein fused to Protein Interacting with C kinase 1 experimental SAS data
CRYSOL model
Sample: Maltose Binding Protein fused to Protein Interacting with C kinase 1 dimer, 174 kDa Homo sapiens protein
Buffer: 50 mM Tris 300 mM NaCl 1 mM maltose 1 mM EGTA 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2015 Oct 13
PICK1 is implicated in organelle motility in an Arp2/3 complex-independent manner. Mol Biol Cell 26(7):1308-22 (2015)
Madasu Y, Yang C, Boczkowska M, Bethoney KA, Zwolak A, Rebowski G, Svitkina T, Dominguez R
RgGuinier 8.4 nm
Dmax 27.6 nm
VolumePorod 483 nm3

SASDLG5 – Human nerve growth factor

Beta-nerve growth factor experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Beta-nerve growth factor dimer, 24 kDa Homo sapiens protein
Buffer: 50 mM Na-phosphate, 1 mM EDTA, pH: 7
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jul 2
The conundrum of the high-affinity NGF binding site formation unveiled? Biophys J 108(3):687-97 (2015)
Covaceuszach S, Konarev PV, Cassetta A, Paoletti F, Svergun DI, Lamba D, Cattaneo A
RgGuinier 2.5 nm

SASDC32 – Ethylene Receptor 1 Cytosolic Domain (in 250 mM NDSB)

Ethylene Receptor 1 experimental SAS data
Ethylene Receptor 1 Cytosolic Domain (in 250 mM NDSB) Rg histogram
Sample: Ethylene Receptor 1 dimer, 129 kDa Arabidopsis thaliana protein
Buffer: 20 mM Tris-NDSB 150 mM NaCl 1mM DTT 250 mM NDSB, pH: 8.8
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 19
Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1). J Biol Chem 290(5):2644-58 (2015)
Mayerhofer H, Panneerselvam S, Kaljunen H, Tuukkanen A, Mertens HD, Mueller-Dieckmann J
RgGuinier 4.7 nm
Dmax 15.8 nm
VolumePorod 316 nm3