Small Angle Scattering Biological Data Bank SASBDB

Browse by MODEL: Ensemble

SASDWS3 – N-acetyl-gamma-glutamyl-phosphate reductase (ArgC)

N-acetyl-gamma-glutamyl-phosphate reductase (ArgC) experimental SAS data

N-acetyl-gamma-glutamyl-phosphate reductase (ArgC) Rg histogram

Sample:	N-acetyl-gamma-glutamyl-phosphate reductase (ArgC) dimer, 97 kDa Paulinella chromatophora protein
Buffer:	20 mM HEPES, 300 mM NaCl, pH: 8
Experiment:	SAXS data collected at Xenocs Xeuss 2.0 Q-Xoom, Center for Structural Studies, Heinrich-Heine-University on 2023 Mar 10

The Paulinella chromatophore transit peptide part2 adopts a structural fold similar to the γ-glutamyl-cyclotransferase fold Plant Physiology (2025)
Klimenko V, Reiners J, Applegate V, Reimann K, Popowicz G, Hoeppner A, Papadopoulos A, Smits S, Nowack E

R_g^Guinier	3.6	nm
D_max	13.1	nm
Volume^Porod	170	nm³

SASDWU3 – RNA helicase (RnaH)

RNA helicase (RnaH) experimental SAS data

Sample:	RNA helicase (RnaH) monomer, 63 kDa Paulinella chromatophora protein
Buffer:	20 mM HEPES, 300 mM NaCl, pH: 8
Experiment:	SAXS data collected at Xenocs Xeuss 2.0 Q-Xoom, Center for Structural Studies, Heinrich-Heine-University on 2024 Oct 28

R_g^Guinier	3.6	nm
D_max	13.7	nm
Volume^Porod	132	nm³

SASDX42 – IgA peptidase (A31-I1166; active site mutant E540A)

IgA protease (E540A) experimental SAS data

IgA peptidase (A31-I1166; active site mutant E540A) Rg histogram

Sample:	IgA protease (E540A) monomer, 128 kDa Thomasclavelia ramosa protein
Buffer:	50 mM Tris, 150 mM NaCl, pH: 8
Experiment:	SAXS data collected at BM29, ESRF on 2023 May 23

Biochemical and structural characterization of the human gut microbiome metallopeptidase IgAse provides insight into its unique specificity for the Fab' region of IgA1 and IgA2. PLoS Pathog 21(7):e1013292 (2025)
Ramírez-Larrota JS, Juyoux P, Guerra P, Eckhard U, Gomis-Rüth FX

R_g^Guinier	5.7	nm
D_max	27.9	nm
Volume^Porod	190	nm³

SASDPP3 – RTX719. Double-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA)

Double-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 experimental SAS data

RTX719. Double-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA) Rg histogram

Sample:	Double-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 monomer, 78 kDa Bordetella pertussis protein
Buffer:	50 mM NaCl, 3 mM CaCl2, 20 mM Tris, pH: 8
Experiment:	SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Feb 15

Acyl chains stabilize the acylated domain and determine the receptor-mediated interaction of the Bordetella adenylate cyclase toxin with cell membrane. J Biol Chem :110392 (2025)
Espinosa-Vinals C, Stransky J, Osicka R, Osickova A, Jurnecka D, Sebo P, Bumba L

R_g^Guinier	3.4	nm
D_max	14.5	nm
Volume^Porod	67	nm³

SASDPQ3 – RTX719-K860R. Mono-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA)

Mono-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 experimental SAS data

RTX719-K860R. Mono-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA) Rg histogram

Sample:	Mono-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 monomer, 78 kDa Bordetella pertussis protein
Buffer:	50 mM NaCl, 3 mM CaCl2, 20 mM Tris, pH: 8
Experiment:	SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Feb 16

R_g^Guinier	5.0	nm
D_max	25.8	nm
Volume^Porod	178	nm³

SASDPR3 – RTX719-K983R. Mono-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA)

RTX719-K983R. Mono-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA) Rg histogram

Sample:	Mono-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 monomer, 78 kDa Bordetella pertussis protein
Buffer:	50 mM NaCl, 3 mM CaCl2, 20 mM Tris, pH: 8
Experiment:	SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Feb 17

R_g^Guinier	5.3	nm
D_max	26.3	nm
Volume^Porod	187	nm³

SASDPS3 – proRTX719. Non-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA)

Non-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 experimental SAS data

proRTX719. Non-acylated truncated variant of B. pertussis adenylate cyclase toxin (CyaA) Rg histogram

Sample:	Non-acylated variant of a genetic fusion comprising the C-terminal folding scaffold of RTX block V (residues 1562–1681 of CyaA) and the CyaA residues 719–1294 monomer, 78 kDa Bordetella pertussis protein
Buffer:	50 mM NaCl, 3 mM CaCl2, 20 mM Tris, pH: 8
Experiment:	SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Feb 22

R_g^Guinier	4.2	nm
D_max	17.8	nm
Volume^Porod	133	nm³

SASDV98 – Full-length N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF

N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF experimental SAS data

Full-length N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF Rg histogram

Sample:	N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF tetramer, 223 kDa Aspergillus fumigatus (strain … protein
Buffer:	50 mM Tris, 200 mM NaCl, pH: 8
Experiment:	SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2022 Jul 7

SidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in Aspergillus fumigatus siderophore biosynthesis Journal of Structural Biology: X 11:100119 (2025)
Poonsiri T, Stransky J, Demitri N, Haas H, Cianci M, Benini S

R_g^Guinier	4.0	nm
D_max	19.0	nm
Volume^Porod	412	nm³

SASDVA8 – The N-terminal domain of N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF

The N-terminal domain of N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF Rg histogram

Sample:	N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF monomer, 25 kDa Aspergillus fumigatus (strain … protein
Buffer:	50 mM Tris, 200 mM NaCl, pH: 8
Experiment:	SAXS data collected at Anton Paar SAXSpoint 2.0, Institute of Biotechnology, Czech Academy of Sciences/Centre of Molecular Structure on 2023 Jan 18

R_g^Guinier	2.2	nm
D_max	8.9	nm
Volume^Porod	30	nm³

SASDSL2 – Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 (EMAPII) at pH 8

Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 experimental SAS data

Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 (EMAPII) at pH 8 Rg histogram

Sample:	Aminoacyl tRNA synthase complex-interacting multifunctional protein 1 monomer, 20 kDa Homo sapiens protein
Buffer:	50 mM Tris, 150 mM NaCl, 1mM DTT, pH: 8
Experiment:	SAXS data collected at Xenocs Xeuss 2.0 with MetalJet, Department of Macromolecular Physics, Faculty of Physics, Adam Mickiewicz University on 2022 Oct 12

Solution structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex
Michal Taube

R_g^Guinier	1.9	nm
D_max	7.7	nm
Volume^Porod	27	nm³

First << Prev Page 3 of 27 Next >> Last