SASBDB entries for UniProt ID:

SASDVK2 – Core domain of human Cathepsin-G, short truncations to both terminus (Δ22-243Δ253)

UniProt ID: P08311 (22-245) Cathepsin G

Cathepsin G experimental SAS data
PHENIX model
Sample: Cathepsin G monomer, 25 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 140 mM NaCl, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2023 Jun 3
S. aureus Eap is a polyvalent inhibitor of neutrophil serine proteases. J Biol Chem 300(9):107627 (2024)
Mishra N, Gido CD, Herdendorf TJ, Hammel M, Hura GL, Fu ZQ, Geisbrecht BV
RgGuinier 1.9 nm
Dmax 6.9 nm
VolumePorod 27 nm3

SASDV33 – N-terminal domain construct of hsGEFH1_190-582aa fit to DAMMIF and Alphafold2 models

UniProt ID: Q92974-1 (190-582) Isoform 1 of Rho guanine nucleotide exchange factor 2

Isoform 1 of Rho guanine nucleotide exchange factor 2 experimental SAS data
ALPHAFOLD model
Sample: Isoform 1 of Rho guanine nucleotide exchange factor 2 monomer, 47 kDa Homo sapiens protein
Buffer: 20mM Tris-Cl, 150mM NaCl, 1mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2021 Feb 19
Structural basis of microtubule-mediated signal transduction. Cell (2025)
Choi SR, Blum TB, Giono M, Roy B, Vakonakis I, Schmid D, Oelgarth N, Ranganathan A, Gossert AD, Shivashankar GV, Zippelius A, Steinmetz MO
RgGuinier 5.9 nm

SASDVB3 – Mononuclear iron bound form of pigeon ISCA1 under geomagnetic condition

UniProt ID: P0DN75 (2-132) Pigeon iron-sulfur cluster assembly 1 homolog, mitochondrial

Pigeon iron-sulfur cluster assembly 1 homolog, mitochondrial experimental SAS data
DAMMIN model
Sample: Pigeon iron-sulfur cluster assembly 1 homolog, mitochondrial, 15 kDa Columba livia protein
Buffer: 20 mM Tris-HCl, 0.15 M NaCl, 10 mM 3-mercapto-1,2-propanediol, pH: 8
Experiment: SAXS data collected at BL-10C, Photon Factory (PF), High Energy Accelerator Research Organization (KEK) on 2021 Jun 8
A hidden property of the iron-sulfur protein in the mononuclear iron-bound state: species-dependent structural ordering induced by magnetic fields. FEBS J (2025)
Arai S, Soga S, Hirai M, Kobayashi R, Masai H, Kimura K, Maeda K, Nagashima H
RgGuinier 2.7 nm
Dmax 7.2 nm
VolumePorod 39 nm3

SASDVJ4 – Complex of CDAN1-interacting nuclease 1 and Codanin1 C-terminal domain (frames 712 - 720)

UniProt ID: Q8IWY9 (1005-1227) Codanin-1

UniProt ID: Q9Y2V0 (1-281) CDAN1-interacting nuclease 1

Codanin-1CDAN1-interacting nuclease 1 experimental SAS data
ALPHAFOLD model
Sample: Codanin-1 monomer, 25 kDa Homo sapiens protein
CDAN1-interacting nuclease 1 monomer, 33 kDa Homo sapiens protein
Buffer: 20 mM Tris HCl, 150 mM NaCl, 5% glycerol, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Sep 29
Anemia-associated mutations disrupt the CDIN1-Codanin1 complex in inherited congenital dyserythropoietic anemia I (CDA-I) disease. FEBS J (2026)
Stojaspal M, Brom T, Nečasová I, Janovič T, Veverka P, Verma N, Uhrík L, Hernychova L, Hofr C
RgGuinier 3.0 nm
Dmax 10.6 nm
VolumePorod 102 nm3

SASDV47 – Peptide-linked fusion protein of Apoptosis-inducing factor 1 AIF(104-613) point mutant W196A and the N-terminal segment of Mitochondrial intermembrane space import and assembly protein 40 CHCHD4(1-45)

UniProt ID: Q8N4Q1 (1-45) Mitochondrial intermembrane space import and assembly protein 40

UniProt ID: O95831 (104-613) Apoptosis-inducing factor 1, mitochondrial

Mitochondrial intermembrane space import and assembly protein 40Apoptosis-inducing factor 1, mitochondrial experimental SAS data
Mitochondrial intermembrane space import and assembly protein 40 Apoptosis-inducing factor 1, mitochondrial Kratky plot
Sample: Mitochondrial intermembrane space import and assembly protein 40 dimer, 12 kDa Homo sapiens protein
Apoptosis-inducing factor 1, mitochondrial dimer, 113 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, 2 mM TCEP, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Nov 28
NADH-bound AIF activates the mitochondrial CHCHD4/MIA40 chaperone by a substrate-mimicry mechanism. EMBO J (2025)
Brosey CA, Shen R, Tainer JA
RgGuinier 3.9 nm
Dmax 12.9 nm
VolumePorod 289 nm3

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

UniProt ID: Q4WF55 (1-462) 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
RgGuinier 4.0 nm
Dmax 19.0 nm
VolumePorod 412 nm3

SASDVZ8 – Pro-Trp-Trp-Pro (PWWP) domain from human DNA (cytosine-5)-methyltransferase 3B (DNMT3B)

UniProt ID: Q9UBC3 (206-355) DNA (cytosine-5)-methyltransferase 3B Pro-Trp-Trp-Pro (PWWP) domain

DNA (cytosine-5)-methyltransferase 3B Pro-Trp-Trp-Pro (PWWP) domain experimental SAS data
GASBOR model
Sample: DNA (cytosine-5)-methyltransferase 3B Pro-Trp-Trp-Pro (PWWP) domain monomer, 17 kDa Homo sapiens protein
Buffer: 20 mM Tris, 300 mM NaCl, 1 mM TCEP, 5% glycerol, pH: 8
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2024 Apr 20
Histone modification-driven structural remodeling unleashes DNMT3B in DNA methylation. Sci Adv 11(13):eadu8116 (2025)
Cho CC, Huang HH, Jiang BC, Yang WZ, Chen YN, Yuan HS
RgGuinier 1.8 nm
Dmax 6.4 nm
VolumePorod 20464 nm3

SASDV99 – Mouse High mobility group protein B2 (HMGB2) apo form

UniProt ID: P30681 (1-210) High mobility group protein B2

High mobility group protein B2 experimental SAS data
Mouse High mobility group protein B2 (HMGB2) apo form Rg histogram
Sample: High mobility group protein B2 monomer, 26 kDa Mus musculus protein
Buffer: Tris 50mM, NaCl 150mM, pH: 7
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2024 Apr 27
High mobility group protein B2 (HMGB2)
Chun I Tu
RgGuinier 2.9 nm
Dmax 10.1 nm
VolumePorod 36 nm3

SASDVF9 – Mouse complex murine Immunoglobulin E (IgE) antibody with profilin

UniProt ID: None (None-None) Murine Immunoglobulin E (IgE) antibodies

UniProt ID: Q9STB6 (1-131) Profilin-2

Murine Immunoglobulin E (IgE) antibodiesProfilin-2 experimental SAS data
DAMFILT model
Sample: Murine Immunoglobulin E (IgE) antibodies monomer, 165 kDa Mus musculus protein
Profilin-2 monomer, 18 kDa Hevea brasiliensis protein
Buffer: 20 mM Tris, 50 mM NaCl, pH: 8.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Oct 3
Allergen-induced structural rearrangements in IgE: insights from SAXS and molecular dynamics. Int J Biol Macromol :147658 (2025)
Gómez-Velasco H, García-Ramírez B, Siliqi D, Graewert MA, Quintero-Martinez A, Ortega E, Rodríguez-Romero A
RgGuinier 6.0 nm
Dmax 19.9 nm
VolumePorod 504 nm3

SASDW92 – 10 mg/mL β-chitin nanofibers from squid pens with 2.5 mg/mL perdeuterated N-acetylglucosamine binding Protein A (D-GbpA) in 47 % D₂O

UniProt ID: None (None-None) β-chitin nanofibers from squid pens

UniProt ID: Q9KLD5 (24-485) GlcNAc-binding protein A (perdeuterated)

β-chitin nanofibers from squid pensGlcNAc-binding protein A (perdeuterated) experimental SAS data
β-chitin nanofibers from squid pens GlcNAc-binding protein A (perdeuterated) Kratky plot
Sample: Β-chitin nanofibers from squid pens None, Squid
GlcNAc-binding protein A (perdeuterated) monomer, 51 kDa Vibrio cholerae serotype … protein
Buffer: 20 mM acetate, 47% v/v D₂O, pH: 5
Experiment: SANS data collected at D11, ILL on 2020 Aug 18
Tangled Up in Fibers: How a Multidomain Lytic Polysaccharide Monooxygenase Binds Its Chitin Substrate. ACS Appl Mater Interfaces (2026)
Sørensen HV, Montserrat-Canals M, Coder A, Prévost S, Krueger S, Vaaje-Kolstad G, Bjerregaard-Andersen K, Lund R, Krengel U