SASBDB entries for UniProt ID:

SASDX72 – Fatty acyl-CoA synthetase FadD5 with 2 mM coenzyme A (CoA)

UniProt ID: O07411 (1-554) Probable fatty-acid-CoA ligase FadD5 (Fatty-acid-CoA synthetase) (Fatty-acid-CoA synthase)
Probable fatty-acid-CoA ligase FadD5 (Fatty-acid-CoA synthetase) (Fatty-acid-CoA synthase) experimental SAS data
ALPHAFOLD model
Sample: Probable fatty-acid-CoA ligase FadD5 (Fatty-acid-CoA synthetase) (Fatty-acid-CoA synthase) dimer, 123 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM HEPES, 500 mM NaCl, 5 mM MgCl2, 1 mM β-mercaptoethanol, 2 mM coenzyme A (CoA), pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2022 Oct 20
Structural enzymological studies of the long chain fatty acyl-CoA synthetase FadD5 from the mce1 operon of Mycobacterium tuberculosis. Biochem Biophys Res Commun 769:151960 (2025)
Rahman MA, Dalwani S, Venkatesan R
RgGuinier 3.7 nm
Dmax 12.0 nm
VolumePorod 210 nm3

SASDXF2 – Probable conserved Mce associated membrane protein (Mam1Adelta106) from M.tuberculosis

UniProt ID: O07419 (107-213) Probable conserved Mce associated membrane protein
Probable conserved Mce associated membrane protein experimental SAS data
ALPHAFOLD model
Sample: Probable conserved Mce associated membrane protein tetramer, 59 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 50mM Tris, 500mM NaCl, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Dec 10
Insight into the structure and interactions of the M. tuberculosis Mce-associated membrane proteins Mam1A-1D (2025)
Hynönen M, Perumal P, Hynönen N, Doutch J, Ma K, Venkatesan R
RgGuinier 3.2 nm
Dmax 90.0 nm
VolumePorod 90 nm3

SASDXG2 – Probable conserved Mce associated membrane protein (Mam1Adelta106) from M.tuberculosis (SANS)

UniProt ID: O07419 (107-213) Probable conserved Mce associated membrane protein
Probable conserved Mce associated membrane protein experimental SAS data
DAMFILT model
Sample: Probable conserved Mce associated membrane protein tetramer, 59 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 50 mM Tris, 500 mM NaCl, D-C12E9, pH: 8.5
Experiment: SANS data collected at SANS2D, ISIS Neutron and Muon Source on 2019 Dec 10
Insight into the structure and interactions of the M. tuberculosis Mce-associated membrane proteins Mam1A-1D (2025)
Hynönen M, Perumal P, Hynönen N, Doutch J, Ma K, Venkatesan R
RgGuinier 2.6 nm
Dmax 8.5 nm
VolumePorod 33 nm3

SASDXW3 – Transthyretin tetramer

UniProt ID: P02766 (21-147) Transthyretin
Transthyretin experimental SAS data
COOT model
Sample: Transthyretin tetramer, 55 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, pH: 7
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2022 Sep 4
Differentiating the solution structures and stability of transthyretin tetramer complexed with tolcapone and tafamidis using SEC-SWAXS and NMR
Orion Shih
RgGuinier 2.4 nm
Dmax 7.2 nm
VolumePorod 92 nm3

SASDXX3 – Transthyretin tetramer with over-saturated tolcapone

UniProt ID: P02766 (21-147) Transthyretin

UniProt ID: None (None-None) Tolcapone
TransthyretinTolcapone experimental SAS data
COOT model
Sample: Transthyretin tetramer, 55 kDa Homo sapiens protein
Tolcapone dimer, 1 kDa
Buffer: 20 mM Tris, 50 mM NaCl, pH: 7
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2023 May 19
Differentiating the solution structures and stability of transthyretin tetramer complexed with tolcapone and tafamidis using SEC-SWAXS and NMR
Orion Shih
RgGuinier 2.5 nm
Dmax 8.6 nm
VolumePorod 107 nm3

SASDXY3 – Transthyretin tetramer with over-saturated tafamidis

UniProt ID: P02766 (21-147) Transthyretin

UniProt ID: None (None-None) Tafamidis
TransthyretinTafamidis experimental SAS data
COOT model
Sample: Transthyretin tetramer, 55 kDa Homo sapiens protein
Tafamidis dimer, 1 kDa
Buffer: 20 mM Tris, 50 mM NaCl, pH: 7
Experiment: SAXS data collected at 13A, Taiwan Photon Source, NSRRC on 2023 May 19
Differentiating the solution structures and stability of transthyretin tetramer complexed with tolcapone and tafamidis using SEC-SWAXS and NMR
Orion Shih
RgGuinier 2.5 nm
Dmax 9.0 nm
VolumePorod 69 nm3

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