Browse by MACROMOLECULE type: protein

SASDFV9 – Adhesion G-protein coupled receptor G6 - zfGpr126 S2 (-ss) D134A/F135A ECR

Adhesion G-protein coupled receptor G6 S2 D134A/F135A experimental SAS data
Adhesion G-protein coupled receptor G6 S2 D134A/F135A Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S2 D134A/F135A monomer, 86 kDa Danio rerio protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
Leon K, Cunningham R, Riback J, Feldman E, Li J, Sosnick T, Zhao M, Monk K, Araç D
RgGuinier 4.3 nm
Dmax 14.8 nm
VolumePorod 181 nm3

SASDFW9 – Adhesion G-protein coupled receptor G6 - hGPR126 S2 (-ss) ECR

Adhesion G-protein coupled receptor G6 S2 experimental SAS data
Adhesion G-protein coupled receptor G6 S2 Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S2 monomer, 88 kDa Homo sapiens protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
Leon K, Cunningham R, Riback J, Feldman E, Li J, Sosnick T, Zhao M, Monk K, Araç D
RgGuinier 4.4 nm
Dmax 15.7 nm
VolumePorod 199 nm3

SASDFX9 – Adhesion G-protein coupled receptor G6 - hGPR126 S1 (+ss) ECR

Adhesion G-protein coupled receptor G6 S1 experimental SAS data
Adhesion G-protein coupled receptor G6 S1 Kratky plot
Sample: Adhesion G-protein coupled receptor G6 S1 monomer, 91 kDa Homo sapiens protein
Buffer: 150 mM NaCl, 20 mM HEPES, pH: 7.5
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Jun 28
Structural basis for adhesion G protein-coupled receptor Gpr126 function Nature Communications 11(1) (2020)
Leon K, Cunningham R, Riback J, Feldman E, Li J, Sosnick T, Zhao M, Monk K, Araç D
RgGuinier 4.9 nm
Dmax 17.1 nm
VolumePorod 213 nm3

SASDGB6 – Resistance to inhibitors of cholinesterase 8 homolog A (Ric8A) miniGi complex

Resistance to inhibitors of cholinesterase 8 homolog AminiGi experimental SAS data
OTHER model
Sample: Resistance to inhibitors of cholinesterase 8 homolog A monomer, 56 kDa Bos taurus protein
MiniGi monomer, 25 kDa synthetic construct protein
Buffer: 20 mM Tris, 150 mM KCl, 5 % glycerol, 1 mM TCEP, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2018 Oct 27
Large-scale conformational rearrangement of the α5-helix of Gα subunits in complex with the guanine nucleotide exchange factor Ric8A. J Biol Chem (2019)
Srivastava D, Artemyev NO
RgGuinier 3.2 nm
Dmax 10.7 nm

SASDFL6 – Adenine specific DNA methyltransferase (Mod Hp_0593) at pH 8

Adenine specific DNA methyltransferase (Mod) experimental SAS data
PYMOL model
Sample: Adenine specific DNA methyltransferase (Mod) dimer, 137 kDa Helicobacter pylori protein
Buffer: 25 mM Tris, 250 mM NaCl, pH: 8
Experiment: SAXS data collected at ID14-3, ESRF on 2017 Jul 9
Tetramerization at low pH licenses DNA methylation activity of M.HpyAXI in the presence of acid stress. J Mol Biol (2019)
Narayanan N, Banerjee A, Jain D, Kulkarni DS, Sharma R, Nirwal S, Rao DN, Nair DT
RgGuinier 3.3 nm
Dmax 12.5 nm
VolumePorod 143 nm3

SASDFM6 – Adenine specific DNA methyltransferase (Mod HP_0593) at pH 5.5

Adenine specific DNA methyltransferase (Mod) experimental SAS data
PYMOL model
Sample: Adenine specific DNA methyltransferase (Mod) tetramer, 273 kDa Helicobacter pylori protein
Buffer: 25 mM citrate, 250 mM NaCl, pH: 5.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Dec 1
Tetramerization at low pH licenses DNA methylation activity of M.HpyAXI in the presence of acid stress. J Mol Biol (2019)
Narayanan N, Banerjee A, Jain D, Kulkarni DS, Sharma R, Nirwal S, Rao DN, Nair DT
RgGuinier 5.0 nm
Dmax 19.1 nm
VolumePorod 316 nm3

SASDFA6 – Proteolytic fragment of phage flagella binding tail protein YSD1_29 (amino acids 373-1296)

Flagella binding tail protein experimental SAS data
DAMMIF model
Sample: Flagella binding tail protein monomer, 103 kDa Salmonella virus Chi protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.03 % NaN3, 5.0 % glycerol, pH: 7.8
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2017 Apr 4
The flagellotropic bacteriophage YSD1 targets Salmonella Typhi with a Chi-like protein tail fibre. Mol Microbiol (2019)
Dunstan RA, Pickard D, Dougan S, Goulding D, Cormie C, Hardy J, Li F, Grinter R, Harcourt K, Yu L, Song J, Schreiber F, Choudhary J, Clare S, Coulibaly F, Strugnell RA, Dougan G, Lithgow T
RgGuinier 5.6 nm
Dmax 27.4 nm
VolumePorod 155 nm3

SASDDR3 – Yeast tRNA Nm34 methyltransferase Trm7-Trm734 complex from Sacharomyces cerevisiae

Trm7: tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferaseTrm734: Regulator of Ty1 transposition protein 10 experimental SAS data
CORAL model
Sample: Trm7: tRNA (cytidine(32)/guanosine(34)-2'-O)-methyltransferase monomer, 36 kDa Saccharomyces cerevisiae protein
Trm734: Regulator of Ty1 transposition protein 10 monomer, 116 kDa Saccharomyces cerevisiae protein
Buffer: 50 mM HEPES, 200 mM KCl, 5% v/v Glycerol, 10mM β-mercaptoethanol, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2015 Dec 16
Structure of tRNA methyltransferase complex of Trm7 and Trm734 reveals a novel binding interface for tRNA recognition. Nucleic Acids Res (2019)
Hirata A, Okada K, Yoshii K, Shiraishi H, Saijo S, Yonezawa K, Shimizu N, Hori H
RgGuinier 3.8 nm
Dmax 13.0 nm
VolumePorod 218 nm3

SASDEV9 – Cytohesin-2; ARF nucleotide-binding site opener, ARNO truncation mutant

Cytohesin-2; ARNO truncation mutant experimental SAS data
DAMMIN model
Sample: Cytohesin-2; ARNO truncation mutant monomer, 40 kDa Homo sapiens protein
Buffer: 300 mM NaCl, 2 mM 2-mercaptoethanol and 30 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at SWING, SOLEIL on 2015 Nov 25
Structural Organization and Dynamics of Homodimeric Cytohesin Family Arf GTPase Exchange Factors in Solution and on Membranes. Structure (2019)
Das S, Malaby AW, Nawrotek A, Zhang W, Zeghouf M, Maslen S, Skehel M, Chakravarthy S, Irving TC, Bilsel O, Cherfils J, Lambright DG
RgGuinier 2.7 nm
Dmax 9.9 nm
VolumePorod 63 nm3

SASDEW9 – Cytohesin-2; ARF nucleotide-binding site opener, ARNO

Cytohesin-2 ARF nucleotide-binding site opener experimental SAS data
GASBOR model
Sample: Cytohesin-2 ARF nucleotide-binding site opener dimer, 93 kDa Homo sapiens protein
Buffer: 300 mM NaCl, 2 mM 2-mercaptoethanol and 30 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Jun 23
Structural Organization and Dynamics of Homodimeric Cytohesin Family Arf GTPase Exchange Factors in Solution and on Membranes. Structure (2019)
Das S, Malaby AW, Nawrotek A, Zhang W, Zeghouf M, Maslen S, Skehel M, Chakravarthy S, Irving TC, Bilsel O, Cherfils J, Lambright DG
RgGuinier 4.8 nm
Dmax 19.7 nm
VolumePorod 145 nm3