SASBDB entries for UniProt ID:

SASDYF7 – Ferric anguibactin-binding protein (FatB) in complex with the ferric catecholate ligand, Fe(3,4-DHB)2

UniProt ID: Q815N5 (None-None) Ferric anguibactin-binding protein
Ferric anguibactin-binding protein experimental SAS data
Ferric anguibactin-binding protein Kratky plot
Sample: Ferric anguibactin-binding protein monomer, 32 kDa Bacillus cereus (strain … protein
Buffer: 20mM Tris-HCl, 100 mM NaCl, pH: 8
Experiment: SAXS data collected at 4C, Pohang Accelerator Laboratory on 2025 Apr 7
Structural basis of FatB-mediated iron uptake via tyrosine/histidine direct coordination accompanying long-distance domain reorganization. Nat Commun (2026)
Lee H, Kim SO, You S, Segalina A, Noh T, Ihee H
RgGuinier 2.1 nm
Dmax 7.1 nm
VolumePorod 42 nm3

SASDZ64 – ABC transporter TM287/288 - heterodimer

UniProt ID: Q9WYC4 (None-None) ABC transporter TM288 subunit

UniProt ID: Q9WYC3 (None-None) ABC transporter, ATP-binding protein
ABC transporter TM288 subunitABC transporter, ATP-binding protein experimental SAS data
ABC transporter TM288 subunit ABC transporter, ATP-binding protein Kratky plot
Sample: ABC transporter TM288 subunit monomer, 68 kDa Thermotoga maritima (strain … protein
ABC transporter, ATP-binding protein monomer, 64 kDa ABC transporter TM287 … protein
Buffer: 20 mM HEPES, 200 mM NaCl, 5 mM MgCl2, 20 μM DMM, 1 mM Mg2+ ATP, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Sep 10
Capturing transient states of heterodimeric ABC transporter TM287/288 by Time-Resolved Small-Angle X-ray Scattering. Biophys J (2026)
Schröder L, De Vecchis D, Gruzinov A, Schäfer LV, Blanchet CE, Seeger MA, Tidow H, Josts I
RgGuinier 5.1 nm

SASDZ74 – ABC transporter TM287/288 heterodimer in complex with nanobody Nb_TM#1

UniProt ID: Q9WYC4 (None-None) ABC transporter TM288 subunit

UniProt ID: Q9WYC3 (None-None) ABC transporter, ATP-binding protein

UniProt ID: None (None-None) Nanobody Nb_TM#1 bound to TM287/288 ABC transporter
ABC transporter TM288 subunitABC transporter, ATP-binding proteinNanobody Nb_TM#1 bound to TM287/288 ABC transporter experimental SAS data
ABC transporter TM288 subunit ABC transporter, ATP-binding protein Nanobody Nb_TM#1 bound to TM287/288 ABC transporter Kratky plot
Sample: ABC transporter TM288 subunit monomer, 68 kDa Thermotoga maritima (strain … protein
ABC transporter, ATP-binding protein monomer, 64 kDa ABC transporter TM287 … protein
Nanobody Nb_TM#1 bound to TM287/288 ABC transporter monomer, 14 kDa Vicugna pacos (alpaca)
Buffer: 20 mM HEPES, 200 mM NaCl, 5 mM MgCl2, 20 μM DMM, 1 mM Mg2+ ATP, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2021 Sep 10
Capturing transient states of heterodimeric ABC transporter TM287/288 by Time-Resolved Small-Angle X-ray Scattering. Biophys J (2026)
Schröder L, De Vecchis D, Gruzinov A, Schäfer LV, Blanchet CE, Seeger MA, Tidow H, Josts I
RgGuinier 5.4 nm

SASDZ84 – ABC transporter TM287/288 heterodimer in presence of Sybody Sb#35

UniProt ID: Q9WYC4 (None-None) ABC transporter TM288 subunit

UniProt ID: Q9WYC3 (None-None) ABC transporter, ATP-binding protein

UniProt ID: None (None-None) Synthetic nanobody Sb_TM#35 bound to TM287/288 ABC transporter
ABC transporter TM288 subunitABC transporter, ATP-binding proteinSynthetic nanobody Sb_TM#35 bound to TM287/288 ABC transporter experimental SAS data
ABC transporter TM288 subunit ABC transporter, ATP-binding protein Synthetic nanobody Sb_TM#35 bound to TM287/288 ABC transporter Kratky plot
Sample: ABC transporter TM288 subunit monomer, 68 kDa Thermotoga maritima (strain … protein
ABC transporter, ATP-binding protein monomer, 64 kDa ABC transporter TM287 … protein
Synthetic nanobody Sb_TM#35 bound to TM287/288 ABC transporter monomer, 14 kDa synthetic (in vitro …
Buffer: 20 mM HEPES, 200 mM NaCl, 5 mM MgCl2, 20 μM DMM, 1 mM Mg2+ ATP, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2023 Jun 6
Capturing transient states of heterodimeric ABC transporter TM287/288 by Time-Resolved Small-Angle X-ray Scattering. Biophys J (2026)
Schröder L, De Vecchis D, Gruzinov A, Schäfer LV, Blanchet CE, Seeger MA, Tidow H, Josts I
RgGuinier 5.4 nm

SASDAC6 – PsrP functional binding region

UniProt ID: A0A0H2URK1 (187-385) Functional binding region (187-385) of the pneumococcal serine-rich repeat protein
Functional binding region (187-385) of the pneumococcal serine-rich repeat protein experimental SAS data
PsrP functional binding region Rg histogram
Sample: Functional binding region (187-385) of the pneumococcal serine-rich repeat protein monomer, 22 kDa Streptococcus pneumoniae protein
Buffer: PBS 5 % Glycerol, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2013 Feb 27
The BR domain of PsrP interacts with extracellular DNA to promote bacterial aggregation; structural insights into pneumococcal biofilm formation. Sci Rep 6:32371 (2016)
Schulte T, Mikaelsson C, Beaussart A, Kikhney A, Deshmukh M, Wolniak S, Pathak A, Ebel C, Löfling J, Fogolari F, Henriques-Normark B, Dufrêne YF, Svergun D, Nygren PÅ, Achour A
RgGuinier 2.0 nm
Dmax 7.8 nm
VolumePorod 38 nm3

SASDAA8 – Chymotrypsinogen A in Tris/HCl

UniProt ID: P00766 (None-None) Chymotrypsinogen A
Chymotrypsinogen A experimental SAS data
CRYSOL model
Sample: Chymotrypsinogen A monomer, 26 kDa Bos taurus protein
Buffer: 100 mM Tris/HCl 100 mM NaCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2006 May 19
Accuracy of molecular mass determination of proteins in solution by small-angle X-ray scattering Journal of Applied Crystallography 40(s1):s245-s249 (2007)
Mylonas E, Svergun D
RgGuinier 1.9 nm
Dmax 5.0 nm

SASDA49 – Cation-free slp-B53

UniProt ID: M4N8T6 (None-None) S-layer protein
S-layer protein experimental SAS data
DAMMIF model
Sample: S-layer protein monomer, 116 kDa Lysinibacillus sphaericus protein
Buffer: Water, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 2
Analysis of self-assembly of S-layer protein slp-B53 from Lysinibacillus sphaericus. Eur Biophys J 46(1):77-89 (2017)
Liu J, Falke S, Drobot B, Oberthuer D, Kikhney A, Guenther T, Fahmy K, Svergun D, Betzel C, Raff J
RgGuinier 5.8 nm
Dmax 22.0 nm
VolumePorod 495 nm3

SASDAA9 – EcPaaA2-EcParE2His construct

UniProt ID: A0A0D7C2L1 (1-92) Plasmid stabilization protein ParE

UniProt ID: A0A0F6F6Q9 (14-75) Uncharacterized protein (Antitoxin)
Plasmid stabilization protein ParE Uncharacterized protein (Antitoxin) experimental SAS data
CRYSOL model
Sample: Plasmid stabilization protein ParE 16-mer, 188 kDa Escherichia coli protein
Uncharacterized protein (Antitoxin) 16-mer, 135 kDa Escherichia coli protein
Buffer: 50 mM Tris-HCl 500 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Dec 9
A unique hetero-hexadecameric architecture displayed by the Escherichia coli O157 PaaA2-ParE2 antitoxin-toxin complex. J Mol Biol 428(8):1589-603 (2016)
Sterckx YG, Jové T, Shkumatov AV, Garcia-Pino A, Geerts L, De Kerpel M, Lah J, De Greve H, Van Melderen L, Loris R
RgGuinier 3.8 nm
Dmax 16.2 nm
VolumePorod 312 nm3

SASDB55 – Glycosylated myelin-associated glycoprotein full extracellular domain (immunoglobulin domains 1-5)

UniProt ID: P20917 (20-508) Myelin-associated glycoprotein Ig domains 1-5
Myelin-associated glycoprotein Ig domains 1-5 experimental SAS data
NONE model
Sample: Myelin-associated glycoprotein Ig domains 1-5 dimer, 108 kDa Mus musculus protein
Buffer: 25 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 11
Structural basis of myelin-associated glycoprotein adhesion and signalling. Nat Commun 7:13584 (2016)
Pronker MF, Lemstra S, Snijder J, Heck AJ, Thies-Weesie DM, Pasterkamp RJ, Janssen BJ
RgGuinier 6.8 nm
Dmax 23.8 nm
VolumePorod 177 nm3

SASDBH6 – Full-length human p23 (1-160)

UniProt ID: Q15185 (1-160) Prostaglandin E synthase 3
Prostaglandin E synthase 3 experimental SAS data
Prostaglandin E synthase 3 Kratky plot
Sample: Prostaglandin E synthase 3 monomer, 19 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 7.5
Experiment: SAXS data collected at SAXS1 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Jun 22
The C-terminal region of the human p23 chaperone modulates its structure and function. Arch Biochem Biophys 565:57-67 (2015)
Seraphim TV, Gava LM, Mokry DZ, Cagliari TC, Barbosa LR, Ramos CH, Borges JC
RgGuinier 2.5 nm
Dmax 10.0 nm
VolumePorod 40 nm3