Browse by MODEL: Hybrid

SASDMY4 – Retinoic acid receptor RXR-alpha DNA binding domain (DBD) in complex with Ramp2

Ramp2 DNARetinoic acid receptor RXR-alpha experimental SAS data
CUSTOM IN-HOUSE model
Sample: Ramp2 DNA monomer, 11 kDa DNA
Retinoic acid receptor RXR-alpha dimer, 20 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 50 mM KCl, 5% glycerol, 2 mM Chaps, and 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Oct 7
Solution Behavior of the Intrinsically Disordered N-Terminal Domain of Retinoid X Receptor α in the Context of the Full-Length Protein Biochemistry 55(12):1741-1748 (2016)
Belorusova A, Osz J, Petoukhov M, Peluso-Iltis C, Kieffer B, Svergun D, Rochel N
RgGuinier 1.9 nm
Dmax 5.8 nm

SASDBR2 – Contactin-associated protein-like 2 (Caspr2) extracellular domains 1-1261.

Contactin-associated protein-like 2 extracellular domains (1-1261) experimental SAS data
DAMMIN model
Sample: Contactin-associated protein-like 2 extracellular domains (1-1261) monomer, 140 kDa Homo sapiens protein
Buffer: 10 mM HEPES 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at Anton Paar SAXSess, University of Utah on 2010 Oct 4
Structural Characterization of the Extracellular Domain of CASPR2 and Insights into Its Association with the Novel Ligand Contactin1. J Biol Chem 291(11):5788-802 (2016)
Rubio-Marrero EN, Vincelli G, Jeffries CM, Shaikh TR, Pakos IS, Ranaivoson FM, von Daake S, Demeler B, De Jaco A, Perkins G, Ellisman MH, Trewhella J, Comoletti D
RgGuinier 4.4 nm
Dmax 14.5 nm
VolumePorod 282 nm3

SASDAX8 – Ribokinase ThiM

Ribokinase ThiM experimental SAS data
CORAL model
Sample: Ribokinase ThiM trimer, 89 kDa Staphylococcus aureus protein
Buffer: 50 mM Potassium phosphate 10 mM MgCl2, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2010 Nov 19
Structure of ThiM from Vitamin B1 biosynthetic pathway of Staphylococcus aureus - Insights into a novel pro-drug approach addressing MRSA infections. Sci Rep 6:22871 (2016)
Drebes J, Künz M, Windshügel B, Kikhney AG, Müller IB, Eberle RJ, Oberthür D, Cang H, Svergun DI, Perbandt M, Betzel C, Wrenger C
RgGuinier 3.0 nm
Dmax 9.0 nm
VolumePorod 145 nm3

SASDAD7 – Structure of a complex between full length and truncated CTP1L endolysin

Endolysin  experimental SAS data
CRYSOL model
Sample: Endolysin , 33 kDa Clostridium phage phiCTP1 protein
Buffer: 20 mM HEPES, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 17
Crystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product. J Biol Chem 291(10):4882-93 (2016)
Dunne M, Leicht S, Krichel B, Mertens HD, Thompson A, Krijgsveld J, Svergun DI, Gómez-Torres N, Garde S, Uetrecht C, Narbad A, Mayer MJ, Meijers R
RgGuinier 3.7 nm
Dmax 13.8 nm
VolumePorod 95 nm3

SASDAE7 – Structure of a complex between full length and truncated CS74L endolysin

Endolysin CS74L  experimental SAS data
DAMMIF model
Sample: Endolysin CS74L , 31 kDa Clostridium phage phi8074-B1 protein
Buffer: 20 mM HEPES, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Mar 17
Crystal Structure of the CTP1L Endolysin Reveals How Its Activity Is Regulated by a Secondary Translation Product. J Biol Chem 291(10):4882-93 (2016)
Dunne M, Leicht S, Krichel B, Mertens HD, Thompson A, Krijgsveld J, Svergun DI, Gómez-Torres N, Garde S, Uetrecht C, Narbad A, Mayer MJ, Meijers R
RgGuinier 3.6 nm
Dmax 14.0 nm
VolumePorod 79 nm3

SASDBS2 – Recombinant Tn antigen-binding lectin from Vatairea macrocarpa

Recombinant Tn antigen-binding lectin experimental SAS data
CORAL model
Sample: Recombinant Tn antigen-binding lectin tetramer, 105 kDa Vatairea macrocarpa protein
Buffer: 100 mM sodium phosphate 150 mM NaCl 5% (v/v) glycerol, pH: 5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2014 Jan 11
Structural characterization of a Vatairea macrocarpa lectin in complex with a tumor-associated antigen: A new tool for cancer research. Int J Biochem Cell Biol 72:27-39 (2016)
Sousa BL, Silva-Filho JC, Kumar P, Graewert MA, Pereira RI, Cunha RMS, Nascimento KS, Bezerra GA, Delatorre P, Djinovic-Carugo K, Nagano CS, Gruber K, Cavada BS
RgGuinier 3.2 nm
Dmax 9.5 nm
VolumePorod 168 nm3

SASDBC3 – RepB, the replication initiator protein of a promiscuous Streptococcal plasmid pMV158

Replication initiator protein of a promiscuous streptococcal plasmid pMV158. experimental SAS data
NONE model
Sample: Replication initiator protein of a promiscuous streptococcal plasmid pMV158. hexamer, Streptococcus sp. protein
Buffer: 10 mM TRIS 5 mM EDTA 1.0 M KCl, pH: 8.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2007 Jun 16
Conformational plasticity of RepB, the replication initiator protein of promiscuous streptococcal plasmid pMV158. Sci Rep 6:20915 (2016)
Boer DR, Ruiz-Masó JA, Rueda M, Petoukhov MV, Machón C, Svergun DI, Orozco M, del Solar G, Coll M
RgGuinier 3.8 nm
Dmax 10.6 nm
VolumePorod 282 nm3

SASDBQ3 – Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164)

Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164) experimental SAS data
DAMMIF model
Sample: Middle East Respiratory Syndrome (MERS) coronavirus nucleocapsid N-Protein (N-terminal domain 1-164) monomer, 18 kDa Middle East respiratory … protein
Buffer: 10 mM HEPES 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2015 Oct 5
Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering. Acta Crystallogr D Struct Biol 72(Pt 2):192-202 (2016)
Papageorgiou N, Lichière J, Baklouti A, Ferron F, Sévajol M, Canard B, Coutard B
RgGuinier 2.0 nm
Dmax 8.0 nm
VolumePorod 28 nm3

SASDL67 – Mutation of the Active Site Residues of Thermus thermophilus 3‑Isopropylmalate Dehydrogenase

3-isopropylmalate dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: 3-isopropylmalate dehydrogenase dimer, 73 kDa Thermus thermophilus protein
Buffer: 25 mM MOPS/NaOH, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2012 Nov 16
Dual Role of the Active Site Residues of Thermus thermophilus 3-Isopropylmalate Dehydrogenase: Chemical Catalysis and Domain Closure. Biochemistry 55(3):560-74 (2016)
Gráczer É, Szimler T, Garamszegi A, Konarev PV, Lábas A, Oláh J, Palló A, Svergun DI, Merli A, Závodszky P, Weiss MS, Vas M
RgGuinier 2.8 nm

SASDBY2 – Inorganic pyrophosphatase (PPase) from E. coli

Inorganic pyrophosphatase (PPase) from E. coli experimental SAS data
DAMMIN model
Sample: Inorganic pyrophosphatase (PPase) from E. coli hexamer, 117 kDa Escherichia coli protein
Buffer: 50 mM Tris 10 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Jun 30
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 3.0 nm
Dmax 9.0 nm
VolumePorod 166 nm3