SASBDB entries for UniProt ID:

SASDLQ4 – Deoxyribose-phosphate aldolase, DeoC

UniProt ID: P0A6L0 (1-259) Deoxyribose-phosphate aldolase
Deoxyribose-phosphate aldolase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Deoxyribose-phosphate aldolase, 28 kDa Escherichia coli (strain … protein
Buffer: 50 mM HEPES, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2019 Oct 1
Protein quaternary structures in solution are a mixture of multiple forms Chemical Science 13(39):11680-11695 (2022)
Marciano S, Dey D, Listov D, Fleishman S, Sonn-Segev A, Mertens H, Busch F, Kim Y, Harvey S, Wysocki V, Schreiber G
RgGuinier 2.6 nm
Dmax 8.0 nm
VolumePorod 61 nm3

SASDL87 – Plasmodium falciparum Glycogen Synthase Kinase 3 - Ion Exchange Chromatography Fraction 4

UniProt ID: O77344 (1-440) Glycogen synthase kinase 3
Glycogen synthase kinase 3 experimental SAS data
CORAL model
Sample: Glycogen synthase kinase 3 monomer, 52 kDa Plasmodium falciparum (isolate … protein
Buffer: 20 mM Tris pH 8.0, 100 mM NaCl, 0.5 mM TCEP, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Nov 19
N-terminal phosphorylation regulates the activity of glycogen synthase kinase 3 from Plasmodium falciparum. Biochem J 479(3):337-356 (2022)
Pazicky S, Alder A, Mertens H, Svergun D, Gilberger T, Löw C
RgGuinier 3.2 nm
Dmax 11.6 nm
VolumePorod 101 nm3

SASDLE8 – The Fe–S cluster assembly 1 homolog of pigeon (Elution No.280)

UniProt ID: P0DN75 (1-132) Iron-sulfur cluster assembly 1 homolog, mitochondrial
Iron-sulfur cluster assembly 1 homolog, mitochondrial experimental SAS data
ROSETTA model
Sample: 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 2020 Feb 25
Magnetic field effects on the structure and molecular behavior of pigeon iron–sulfur protein Protein Science 31(6) (2022)
Arai S, Shimizu R, Adachi M, Hirai M
RgGuinier 2.2 nm

SASDLC9 – 2-aminomuconic 6-semialdehyde dehydrogenase double truncation mutant (Δ124-138; Δ477-491)

UniProt ID: Q9KWS5 (1-476) 2-aminomuconic 6-semialdehyde dehydrogenase
2-aminomuconic 6-semialdehyde dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: 2-aminomuconic 6-semialdehyde dehydrogenase dimer, 101 kDa Pseudomonas sp. protein
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7
Experiment: SAXS data collected at BL19U2, Shanghai Synchrotron Radiation Facility (SSRF) on 2021 Feb 1
The tetrameric assembly of 2-aminomuconic 6-semialdehyde dehydrogenase is a functional requirement of cofactor NAD(+) binding. Environ Microbiol 24(7):2994-3012 (2022)
Shi Q, Chen Y, Li X, Dong H, Chen C, Zhong Z, Yang C, Liu G, Su D
RgGuinier 2.9 nm
Dmax 9.0 nm
VolumePorod 117 nm3

SASDMQ5 – Bacillus subtilis complex of diadenylate cyclase (CdaA:cytoplasmic domain) in complex with a truncated version of phosphoglucosamine mutase (GlmMF369)

UniProt ID: Q45589 (97-273) Cyclic di-AMP synthase CdaA

UniProt ID: O34824 (1-369) Phosphoglucosamine mutase
Cyclic di-AMP synthase CdaAPhosphoglucosamine mutase experimental SAS data
Cyclic di-AMP synthase CdaA Phosphoglucosamine mutase Kratky plot
Sample: Cyclic di-AMP synthase CdaA dimer, 44 kDa Bacillus subtilis (strain … protein
Phosphoglucosamine mutase dimer, 83 kDa Bacillus subtilis protein
Buffer: 30 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2021 Aug 2
Structural basis for the inhibition of the Bacillus subtilis c-di-AMP cyclase CdaA by the phosphoglucomutase GlmM Journal of Biological Chemistry :101317 (2021)
Pathania M, Tosi T, Millership C, Hoshiga F, Morgan R, Freemont P, Gründling A
RgGuinier 3.7 nm
Dmax 15.1 nm
VolumePorod 156 nm3

SASDM57 – NAD glycohydrolase (NADase)/Streptolysin O (SLO) complex (SAXS with additional contrast variation SANS data)

UniProt ID: J7M2L4 (41-454) NAD glycohydrolase

UniProt ID: P0C0I3 (32-571) Streptolysin O (T66M)
NAD glycohydrolaseStreptolysin O (T66M) experimental SAS data
BILBOMD model
Sample: NAD glycohydrolase monomer, 47 kDa Streptococcus pyogenes M1 … protein
Streptolysin O (T66M) monomer, 63 kDa Streptococcus pyogenes serotype … protein
Buffer: phosphate buffered saline, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Oct 16
Structural basis underlying the synergism of NADase and SLO during group A Streptococcus infection. Commun Biol 6(1):124 (2023)
Tsai WJ, Lai YH, Shi YA, Hammel M, Duff AP, Whitten AE, Wilde KL, Wu CM, Knott R, Jeng US, Kang CY, Hsu CY, Wu JL, Tsai PJ, Chiang-Ni C, Wu JJ, Lin YS, Liu CC, Senda T, Wang S
RgGuinier 4.8 nm
Dmax 18.4 nm
VolumePorod 125 nm3

SASDME7 – ESX-1 secretion-associated protein EspB medium construct

UniProt ID: P9WJD9 (2-348) ESX-1 secretion-associated protein EspB
ESX-1 secretion-associated protein EspB experimental SAS data
ESX-1 secretion-associated protein EspB Kratky plot
Sample: ESX-1 secretion-associated protein EspB monomer, 37 kDa Mycobacterium tuberculosis (strain … protein
Buffer: 20 mM Tris-HCl, 300 mM NaCl, pH: 8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2018 Sep 21
The crystal structure of the EspB-EspK virulence factor-chaperone complex suggests an additional type VII secretion mechanism in M. tuberculosis. J Biol Chem :102761 (2022)
Gijsbers A, Eymery M, Gao Y, Menart I, Vinciauskaite V, Siliqi D, Peters PJ, McCarthy A, Ravelli RBG
RgGuinier 3.5 nm
Dmax 13.3 nm
VolumePorod 75 nm3

SASDMN7 – Apo-serotransferrin at pH 7.0

UniProt ID: P02787 (1-698) Serotransferrin
Serotransferrin experimental SAS data
GASBOR model
Sample: Serotransferrin monomer, 77 kDa Homo sapiens protein
Buffer: 15 mM HEPES, 20 mM NaHCO3, 50 mM NaCl (APO Buffer), pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2021 Apr 7
X-ray Characterization of Conformational Changes of Human Apo- and Holo-Transferrin International Journal of Molecular Sciences 22(24):13392 (2021)
Campos-Escamilla C, Siliqi D, Gonzalez-Ramirez L, Lopez-Sanchez C, Gavira J, Moreno A
RgGuinier 3.1 nm
Dmax 9.6 nm
VolumePorod 106 nm3

SASDMW8 – The disulphide-linked tetramer of splicing factor, proline- and glutamine-rich and Non-POU domain-containing octamer-binding protein (SFPQ276-598(R542C)/NONO53-312) at 0.78mg/ml

UniProt ID: Q15233 (53-312) Non-POU domain-containing octamer-binding protein

UniProt ID: P23246 (276-598) Splicing factor, proline- and glutamine-rich SFPQ276-598(R542C)/NONO53-312 dimer)
Non-POU domain-containing octamer-binding proteinSplicing factor, proline- and glutamine-rich SFPQ276-598(R542C)/NONO53-312 dimer) experimental SAS data
DAMMIF model
Sample: Non-POU domain-containing octamer-binding protein dimer, 60 kDa Homo sapiens protein
Splicing factor, proline- and glutamine-rich SFPQ276-598(R542C)/NONO53-312 dimer) dimer, 76 kDa Homo sapiens protein
Buffer: 20 mM Tris, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Apr 28
Structural plasticity of the coiled-coil interactions in human SFPQ. Nucleic Acids Res (2024)
Koning HJ, Lai JY, Marshall AC, Stroeher E, Monahan G, Pullakhandam A, Knott GJ, Ryan TM, Fox AH, Whitten A, Lee M, Bond CS
RgGuinier 5.2 nm
Dmax 21.0 nm
VolumePorod 257 nm3

SASDMF9 – 7SK small nuclear RNA stem loop-1 bound to the arginine rich motif of HIV-1 Tat Group M, Subtype B (Isolate A18188)

UniProt ID: None (44-60) Protein Tat

UniProt ID: None (None-None) Homo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNA
Protein TatHomo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNA experimental SAS data
Protein Tat Homo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNA Kratky plot
Sample: Protein Tat monomer, 2 kDa Human immunodeficiency virus … protein
Homo sapiens RNA component of 7SK nuclear ribonucleoprotein (RN7SK), small nuclear RNA monomer, 18 kDa Homo sapiens RNA
Buffer: 10 mM phosphate, 70 mM NaCl, 0.1 mM EDTA, pH: 5.6
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Sep 9
A structure-based mechanism for displacement of the HEXIM adapter from 7SK small nuclear RNA. Commun Biol 5(1):819 (2022)
Pham VV, Gao M, Meagher JL, Smith JL, D'Souza VM
RgGuinier 2.3 nm
Dmax 9.7 nm
VolumePorod 28 nm3