SASBDB entries for UniProt ID:

SASDLR4 – 3-oxoacyl-[acyl-carrier-protein] reductase, FabG

UniProt ID: P0AEK2 (1-244) 3-oxoacyl-[acyl-carrier-protein] reductase FabG
3-oxoacyl-[acyl-carrier-protein] reductase FabG experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: 3-oxoacyl-[acyl-carrier-protein] reductase FabG, 26 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 3.6 nm
Dmax 10.6 nm
VolumePorod 212 nm3

SASDL25 – Bacillus subtilis complex of diadenylate cyclase (CdaA:cytoplasmic domain) and phosphoglucosamine mutase (GlmM)

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

UniProt ID: O34824 (1-448) 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, 101 kDa Bacillus subtilis (strain … protein
Buffer: 30 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 Jul 21
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 4.5 nm
Dmax 16.2 nm
VolumePorod 250 nm3

SASDL56 – 14-3-3 zeta truncated at C-terminus

UniProt ID: P63104 (None-None) 14-3-3 protein zeta/delta
14-3-3 protein zeta/delta experimental SAS data
14-3-3 protein zeta/delta Kratky plot
Sample: 14-3-3 protein zeta/delta dimer, 53 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Oct 13
A structural study of the cytoplasmic chaperone effect of 14-3-3 proteins on Ataxin-1. J Mol Biol :167174 (2021)
Leysen S, Jane Burnley R, Rodriguez E, Milroy LG, Soini L, Adamski CJ, Nitschke L, Davis R, Obsil T, Brunsveld L, Crabbe T, Yahya Zoghbi H, Ottmann C, Martin Davis J
RgGuinier 2.8 nm
Dmax 7.9 nm

SASDLD8 – The Fe–S cluster assembly 1 homolog of pigeon (Elution No.270)

UniProt ID: P0DN75 (2-132) 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

SASDLD9 – 2-aminomuconic 6-semialdehyde dehydrogenase wild-type

UniProt ID: Q9KWS5 (1-491) 2-aminomuconic 6-semialdehyde dehydrogenase
2-aminomuconic 6-semialdehyde dehydrogenase experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: 2-aminomuconic 6-semialdehyde dehydrogenase tetramer, 215 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 3.9 nm
Dmax 11.6 nm
VolumePorod 326 nm3

SASDM47 – NAD glycohydrolase (NADase)

UniProt ID: J7M2L4 (41-454) NAD glycohydrolase
NAD glycohydrolase experimental SAS data
BILBOMD model
Sample: NAD glycohydrolase monomer, 47 kDa Streptococcus pyogenes M1 … 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 3.0 nm
Dmax 103.0 nm
VolumePorod 66 nm3

SASDMD7 – ESX-1 secretion-associated protein EspB large construct

UniProt ID: P9WJD9 (2-460) 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, 48 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 5.0 nm
Dmax 19.2 nm
VolumePorod 119 nm3

SASDMP7 – Apo-serotransferrin at pH 8.0

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 (Buffer APO-Tf-1), pH: 8
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 9.4 nm
VolumePorod 106 nm3

SASDMV7 – The tetramer of splicing factor, proline- and glutamine-rich and Non-POU domain-containing octamer-binding protein (SFPQ214-598(R542C)/NONO53-312)

UniProt ID: P23246 (214-707) Splicing factor, proline- and glutamine-rich

UniProt ID: Q15233 (53-312) Non-POU domain-containing octamer-binding protein
Splicing factor, proline- and glutamine-richNon-POU domain-containing octamer-binding protein experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Splicing factor, proline- and glutamine-rich dimer, 153 kDa Homo sapiens protein
Non-POU domain-containing octamer-binding protein dimer, 60 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 7.5, 250 mM NaCl, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 18
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 5.5 nm
Dmax 20.4 nm
VolumePorod 304 nm3

SASDMC9 – Plasmodium falciparum Glycogen Synthase Kinase 3 - Ion Exchange Chromatography Fraction 1

UniProt ID: O77344 (1-440) Glycogen synthase kinase 3
Glycogen synthase kinase 3 experimental SAS data
ROSETTA 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 3.3 nm
Dmax 13.0 nm
VolumePorod 102 nm3