SASBDB entries for UniProt ID:

SASDHW7 – RnlA-RnlB toxin-antitoxin complex (mRNA endoribonuclease toxin LS : Antitoxin RnlB)

UniProt ID: P52129 (1-357) mRNA endoribonuclease toxin LS

UniProt ID: P52130 (1-123) Antitoxin RnlB (C-terminal His-tagged)
mRNA endoribonuclease toxin LSAntitoxin RnlB (C-terminal His-tagged) experimental SAS data
mRNA endoribonuclease toxin LS Antitoxin RnlB (C-terminal His-tagged) Kratky plot
Sample: MRNA endoribonuclease toxin LS dimer, 80 kDa Escherichia coli protein
Antitoxin RnlB (C-terminal His-tagged) monomer, 15 kDa Escherichia coli protein
Buffer: 20 mM Tris, 150 mM NaCl, 1 mM TCEP, 5% glycerol, pH: 8
Experiment: SAXS data collected at BM29, ESRF on 2018 Jul 25
Alternative dimerization is required for activity and inhibition of the HEPN ribonuclease RnlA Nucleic Acids Research 49(12):7164-7178 (2021)
Garcia-Rodriguez G, Charlier D, Wilmaerts D, Michiels J, Loris R
RgGuinier 3.5 nm
Dmax 10.0 nm
VolumePorod 161 nm3

SASDH79 – Human Cation-independent mannose-6-phosphate receptor domains 9-10

UniProt ID: P11717 (1222-1510) Cation-independent mannose-6-phosphate receptor
Cation-independent mannose-6-phosphate receptor experimental SAS data
MULTIFOXS model
Sample: Cation-independent mannose-6-phosphate receptor dimer, 67 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2020 Jan 25
Structure of the Human Cation-Independent Mannose 6-Phosphate/IGF2 Receptor Domains 7–11 Uncovers the Mannose 6-Phosphate Binding Site of Domain 9 Structure (2020)
Bochel A, Williams C, McCoy A, Hoppe H, Winter A, Nicholls R, Harlos K, Jones E, Berger I, Hassan A, Crump M
RgGuinier 3.3 nm
Dmax 9.2 nm
VolumePorod 93 nm3

SASDH89 – Mitochondrial TIM8·13 chaperone in complex with the Tim23 membrane protein precursor

UniProt ID: P57744 (None-None) Mitochondrial import inner membrane translocase subunit TIM8

UniProt ID: P53299 (None-None) Mitochondrial import inner membrane translocase subunit TIM13

UniProt ID: P32897 (None-None) Mitochondrial import inner membrane translocase subunit TIM23
Mitochondrial import inner membrane translocase subunit TIM8Mitochondrial import inner membrane translocase subunit TIM13Mitochondrial import inner membrane translocase subunit TIM23 experimental SAS data
CUSTOM IN-HOUSE model
Sample: Mitochondrial import inner membrane translocase subunit TIM8 trimer, 29 kDa Saccharomyces cerevisiae protein
Mitochondrial import inner membrane translocase subunit TIM13 trimer, 34 kDa Saccharomyces cerevisiae protein
Mitochondrial import inner membrane translocase subunit TIM23 monomer, 24 kDa Saccharomyces cerevisiae protein
Buffer: 50 mM Tris, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2015 Apr 24
Structural basis of client specificity in mitochondrial membrane-protein chaperones. Sci Adv 6(51) (2020)
Sučec I, Wang Y, Dakhlaoui O, Weinhäupl K, Jores T, Costa D, Hessel A, Brennich M, Rapaport D, Lindorff-Larsen K, Bersch B, Schanda P
RgGuinier 3.1 nm
Dmax 11.3 nm

SASDHY9 – Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein (amino acids 38-408): DHPH

UniProt ID: Q8TCU6 (38-408) Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein experimental SAS data
Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein (amino acids 38-408): DHPH Rg histogram
Sample: Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein monomer, 43 kDa Homo sapiens protein
Buffer: 20 mM HEPES, 300mM NaCl, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2019 Oct 19
The first DEP domain of the RhoGEF P-Rex1 autoinhibits activity andcontributes to membrane binding. J Biol Chem (2020)
Ravala SK, Hopkins JB, Plescia CB, Allgood SR, Kane MA, Cash JN, Stahelin RV, Tesmer JJG
RgGuinier 2.8 nm
Dmax 10.5 nm
VolumePorod 64 nm3

SASDJN2 – Tyrosyl-DNA phosphodiesterase 1 (TDP1)

UniProt ID: Q9NUW8 (1-608) Tyrosyl-DNA phosphodiesterase 1
Tyrosyl-DNA phosphodiesterase 1 experimental SAS data
BILBOMD model
Sample: Tyrosyl-DNA phosphodiesterase 1 monomer, 71 kDa Homo sapiens protein
Buffer: 200 mM NaCl, 20 mM Tris-HCl, pH 7.5, 2% glycerol,, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Jun 26
Direct interaction of DNA repair protein tyrosyl DNA phosphodiesterase 1 and the DNA ligase III catalytic domain is regulated by phosphorylation of its flexible N-terminus. J Biol Chem :100921 (2021)
Rashid I, Hammel M, Sverzhinsky A, Tsai MS, Pascal JM, Tainer JA, Tomkinson AE
RgGuinier 3.2 nm
Dmax 11.7 nm
VolumePorod 143 nm3

SASDJV4 – X-ray repair cross-complementing proteins 5ΔCTR and 6

UniProt ID: P12956 (1-609) X-ray repair cross-complementing protein 6

UniProt ID: P13010 (1-565) X-ray repair cross-complementing protein 5 ΔCTR
X-ray repair cross-complementing protein 6X-ray repair cross-complementing protein 5 ΔCTR experimental SAS data
BILBOMD model
Sample: X-ray repair cross-complementing protein 6 monomer, 70 kDa Homo sapiens protein
X-ray repair cross-complementing protein 5 ΔCTR monomer, 64 kDa Homo sapiens protein
Buffer: 50 mM Hepes, 50 mM KCl, 5 mM MgCl2, 5% glycerol and 0.2 mM DTT, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 Mar 12
Visualizing functional dynamicity in the DNA-dependent protein kinase holoenzyme DNA-PK complex by integrating SAXS with cryo-EM. Prog Biophys Mol Biol (2020)
Hammel M, Rosenberg DJ, Bierma J, Hura GL, Lees-Miller SP, Tainer JA
RgGuinier 3.8 nm
Dmax 12.5 nm
VolumePorod 240 nm3

SASDJF5 – SUN domain of SUN1 harbouring mutation I673E - monomer

UniProt ID: O94901 (616-812) SUN domain-containing protein 1, I673E
SUN domain-containing protein 1, I673E experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: SUN domain-containing protein 1, I673E monomer, 23 kDa Homo sapiens protein
Buffer: 20 mM Tris pH 8.0, 150 mM KCl, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2017 Jul 29
A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies. Elife 10 (2021)
Gurusaran M, Davies OR
RgGuinier 2.1 nm
Dmax 8.2 nm
VolumePorod 42 nm3

SASDJE6 – Metallothionein (MT) 2 protein from the plant Cicer arietinum

UniProt ID: Q39459 (2-79) Metallothionein-like protein 2
Metallothionein-like protein 2 experimental SAS data
Metallothionein (MT) 2 protein from the plant Cicer arietinum Rg histogram
Sample: Metallothionein-like protein 2 monomer, 8 kDa Cicer arietinum protein
Buffer: 10 mM Tris, 50 mM NaCl, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Aug 8
Structural Characterization of Plant Metallothionein
Dima Molodenskiy
RgGuinier 1.9 nm
Dmax 7.3 nm
VolumePorod 5 nm3

SASDJU9 – Mammalian cell entry protein 1A (Mce1A36-148)

UniProt ID: Q79FZ9 (36-148) Mce-family protein Mce1A monomer
Mce-family protein Mce1A monomer experimental SAS data
DAMMIN model
Sample: Mce-family protein Mce1A monomer monomer, 17 kDa Mycobacterium tuberculosis protein
Buffer: 50 mM Tris, 350 mM NaCl, 10% Glycerol, pH: 8.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 May 10
Structural insights into the substrate-binding proteins Mce1A and Mce4A from Mycobacterium tuberculosis IUCrJ 8(5) (2021)
Asthana P, Singh D, Pedersen J, Hynönen M, Sulu R, Murthy A, Laitaoja M, Jänis J, Riley L, Venkatesan R
RgGuinier 2.1 nm
Dmax 8.7 nm
VolumePorod 29 nm3

SASDK42 – Chitin-binding protein CbpD (Pseudomonas aeruginosa), ESRF BM29 data

UniProt ID: Q9I589 (26-389) Chitin-binding protein CbpD
Chitin-binding protein CbpD experimental SAS data
OTHER model
Sample: Chitin-binding protein CbpD monomer, 39 kDa Pseudomonas aeruginosa protein
Buffer: 15 mM Tris-HCl 150 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2020 Oct 1
The lytic polysaccharide monooxygenase CbpD promotes Pseudomonas aeruginosa virulence in systemic infection. Nat Commun 12(1):1230 (2021)
Askarian F, Uchiyama S, Masson H, Sørensen HV, Golten O, Bunæs AC, Mekasha S, Røhr ÅK, Kommedal E, Ludviksen JA, Arntzen MØ, Schmidt B, Zurich RH, van Sorge NM, Eijsink VGH, Krengel U, Mollnes TE, Lewis NE, Nizet V, Vaaje-Kolstad G
RgGuinier 3.2 nm
Dmax 12.0 nm
VolumePorod 64131 nm3