SASBDB entries for UniProt ID:

SASDYF4 – Mutant Elongation Factor Like-1 protein

UniProt ID: P53893 (1-1110) Mutated ribosome assembly protein 1 (R1086Q) with C-terminal tag (RSRSGSENLYFQGSHHHHHHHH)
Mutated ribosome assembly protein 1 (R1086Q) with C-terminal tag (RSRSGSENLYFQGSHHHHHHHH) experimental SAS data
Mutated ribosome assembly protein 1 (R1086Q) with C-terminal tag (RSRSGSENLYFQGSHHHHHHHH) Kratky plot
Sample: Mutated ribosome assembly protein 1 (R1086Q) with C-terminal tag (RSRSGSENLYFQGSHHHHHHHH) monomer, 127 kDa Saccharomyces cerevisiae protein
Buffer: 50 mM HEPES, 300 mM NaCl, 5 mM MgCl2, 5% glycerol, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2024 Oct 3
Hydroxyl radical footprinting modification reveals an intradomain communication pathway in EFL1 disrupted by a Shwachman-Diamond syndrome-associated mutation. Protein Sci 35(4):e70504 (2026)
Zúñiga-Domínguez JA, Jain R, González-Andrade M, Farquhar ER, Chance MR, Gijsbers A, Sánchez-Puig N
RgGuinier 4.7 nm
Dmax 15.2 nm
VolumePorod 314 nm3

SASDA68 – Aldolase in Tris/HCl

UniProt ID: P00883 (2-364) Fructose-bisphosphate aldolase A
Fructose-bisphosphate aldolase A experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Fructose-bisphosphate aldolase A tetramer, 157 kDa Oryctolagus cuniculus 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 3.6 nm
Dmax 10.5 nm

SASDA69 – slp-B53 with Mg2+

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 with Mg2+, pH:
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 6.6 nm
Dmax 29.0 nm
VolumePorod 597 nm3

SASDB36 – Glycosylated myelin-associated glycoprotein full extracellular domain (Ig1-5) N406Q mutant

UniProt ID: P20917 (20-508) Myelin-associated glycoprotein (20-508; N406Q mutant)
Myelin-associated glycoprotein (20-508; N406Q mutant) experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Myelin-associated glycoprotein (20-508; N406Q mutant) monomer, 54 kDa Mus musculus protein
Buffer: 20 mM HEPES 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 5
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 7.3 nm
Dmax 25.6 nm
VolumePorod 193 nm3

SASDBL6 – Truncated construct of human p23 (1-117)

UniProt ID: Q15185 (1-117) Prostaglandin E synthase 3 (1-117)
Prostaglandin E synthase 3 (1-117) experimental SAS data
Prostaglandin E synthase 3 (1-117) Kratky plot
Sample: Prostaglandin E synthase 3 (1-117) monomer, 14 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 2013 Jun 21
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 1.9 nm
Dmax 7.0 nm
VolumePorod 29 nm3

SASDBQ6 – Nucleolysin TIA-1 isoform p40 in complex with TTTTTACTCC DNA

UniProt ID: P31483-2 (93-274) Nucleolysin TIA-1 isoform p40

UniProt ID: (None-None) DNA (TTTTTACTCC)
Nucleolysin TIA-1 isoform p40DNA (TTTTTACTCC) experimental SAS data
Nucleolysin TIA-1 isoform p40 DNA (TTTTTACTCC) Kratky plot
Sample: Nucleolysin TIA-1 isoform p40 monomer, 21 kDa Homo sapiens protein
DNA (TTTTTACTCC) monomer, 1 kDa DNA
Buffer: 20 mM HEPES, 100 mM NaCl, 3% v/v glycerol, pH: 7
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 May 27
TIA-1 RRM23 binding and recognition of target oligonucleotides. Nucleic Acids Res 45(8):4944-4957 (2017)
Waris S, García-Mauriño SM, Sivakumaran A, Beckham SA, Loughlin FE, Gorospe M, Díaz-Moreno I, Wilce MCJ, Wilce JA
RgGuinier 2.1 nm
Dmax 7.1 nm
VolumePorod 32 nm3

SASDBB7 – Human NEI like DNA glycosylase 1 (NEIL1) bound to DNA

UniProt ID: Q96FI4 (None-None) Endonuclease 8-like 1

UniProt ID: (None-None) dsDNA
Endonuclease 8-like 1dsDNA experimental SAS data
DAMMIN model
Sample: Endonuclease 8-like 1 monomer, 45 kDa Homo sapiens protein
DsDNA monomer, 2 kDa DNA
Buffer: 25mM HEPES 100mM NaCl 1mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Jan 20
Destabilization of the PCNA trimer mediated by its interaction with the NEIL1 DNA glycosylase. Nucleic Acids Res 45(5):2897-2909 (2017)
Prakash A, Moharana K, Wallace SS, Doublié S
RgGuinier 3.3 nm
Dmax 17.5 nm
VolumePorod 92 nm3

SASDBF7 – Dps2, DNA binding protein under starvation conditions (SEC-SAXS)

UniProt ID: Q9RZN1 (31-241) N-terminal truncated DNA protection during starvation protein 2
N-terminal truncated DNA protection during starvation protein 2 experimental SAS data
EOM/RANCH model
Sample: N-terminal truncated DNA protection during starvation protein 2 dodecamer, 279 kDa Deinococcus radiodurans R1 protein
Buffer: 20 mM Tris-HCl, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2013 Nov 22
SAXS Structural Studies of Dps from Deinococcus radiodurans Highlights the Conformation of the Mobile N-Terminal Extensions. J Mol Biol 429(5):667-687 (2017)
Santos SP, Cuypers MG, Round A, Finet S, Narayanan T, Mitchell EP, Romão CV
RgGuinier 4.2 nm
Dmax 12.7 nm
VolumePorod 445 nm3

SASDB48 – Major viral transcription factor ICP4/Immediate Early 3 DNA (ICP4N IE3_19mer) complex

UniProt ID: P08392 (258-487) Major viral transcription factor ICP4

UniProt ID: (None-None) Immediate Early 3
Major viral transcription factor ICP4Immediate Early 3 experimental SAS data
NONE model
Sample: Major viral transcription factor ICP4 dimer, 49 kDa Human alphaherpesvirus 1 protein
Immediate Early 3 dimer, 12 kDa DNA
Buffer: 20 mM HEPES, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at B21, Diamond Light Source on 2015 Jul 27
The herpes viral transcription factor ICP4 forms a novel DNA recognition complex. Nucleic Acids Res 45(13):8064-8078 (2017)
Tunnicliffe RB, Lockhart-Cairns MP, Levy C, Mould AP, Jowitt TA, Sito H, Baldock C, Sandri-Goldin RM, Golovanov AP
RgGuinier 2.5 nm
Dmax 8.3 nm
VolumePorod 90 nm3

SASDBX9 – Immunoglobulin domain 6 of Nucleoporin Pom152 (Pom152 Ig-6: amino acids 919-1020)

UniProt ID: P39685 (None-None) Nucleoporin POM152
Nucleoporin POM152 experimental SAS data
DAMMIN model
Sample: Nucleoporin POM152 monomer, 12 kDa Saccharomyces cerevisiae protein
Buffer: 10mM HEPES, 150mM NaCl, 10%(v/v) glycerol, 5mM DTT, pH: 7.5
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2015 Apr 12
Molecular Architecture of the Major Membrane Ring Component of the Nuclear Pore Complex. Structure 25(3):434-445 (2017)
Upla P, Kim SJ, Sampathkumar P, Dutta K, Cahill SM, Chemmama IE, Williams R, Bonanno JB, Rice WJ, Stokes DL, Cowburn D, Almo SC, Sali A, Rout MP, Fernandez-Martinez J
RgGuinier 2.8 nm
Dmax 7.9 nm
VolumePorod 57 nm3