SASBDB entries for UniProt ID:

SASDJX4 – DNA-dependent protein kinase catalytic subunit (DNA-PKcs)

UniProt ID: P78527 (10-4128) DNA-dependent protein kinase catalytic subunit
DNA-dependent protein kinase catalytic subunit experimental SAS data
BILBOMD model
Sample: DNA-dependent protein kinase catalytic subunit monomer, 468 kDa Homo sapiens protein
Buffer: 50 mM Tris-HCl, 100 mM NaCl, 5% glycerol, 0.01% sodium azide, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2016 Dec 30
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 5.6 nm
Dmax 15.6 nm
VolumePorod 1040 nm3

SASDJE5 – LINC complex between the SUN domain of SUN1 and KASH domain of Nesprin-1 - SUN1-KASH1 6:6 complex

UniProt ID: O94901 (616-812) SUN domain-containing protein 1

UniProt ID: Q8NF91 (8769-8797) Nesprin-1
SUN domain-containing protein 1Nesprin-1 experimental SAS data
CORAL model
Sample: SUN domain-containing protein 1 hexamer, 135 kDa Homo sapiens protein
Nesprin-1 hexamer, 22 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 Dec 17
A molecular mechanism for LINC complex branching by structurally diverse SUN-KASH 6:6 assemblies. Elife 10 (2021)
Gurusaran M, Davies OR
RgGuinier 3.9 nm
Dmax 13.0 nm
VolumePorod 254 nm3

SASDJZ9 – Mammalian cell entry protein 1A (Mce1A38-325)

UniProt ID: Q79FZ9 (38-325) Mce-family protein Mce1A

UniProt ID: None (None-None) n-Dodecyl-β-D-Maltopyranoside
Mce-family protein Mce1An-Dodecyl-β-D-Maltopyranoside experimental SAS data
CUSTOM IN-HOUSE model
Sample: Mce-family protein Mce1A monomer, 36 kDa Mycobacterium tuberculosis protein
N-Dodecyl-β-D-Maltopyranoside 0, 82 kDa
Buffer: 50 mM Tris, 500 mM NaCl, 10% Glycerol, 5 mM DDM, 1 mM β-ME, pH: 7.5
Experiment: SAXS data collected at B21, Diamond Light Source on 2019 May 2
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 4.6 nm
Dmax 17.5 nm
VolumePorod 151 nm3

SASDK47 – SANS data for the sensory rhodopsin II / transducer complex in detergent at 1.4 M NaCl

UniProt ID: P42196 (1-239) Sensory rhodopsin II from Natronbacterium pharaonis

UniProt ID: P42259 (3-534) Sensory rhodopsin II transducer from Natronomonas pharaonis
Sensory rhodopsin II from Natronbacterium pharaonisSensory rhodopsin II transducer from Natronomonas pharaonis experimental SAS data
MEMPROT model
Sample: Sensory rhodopsin II from Natronbacterium pharaonis dimer, 53 kDa Natronomonas pharaonis protein
Sensory rhodopsin II transducer from Natronomonas pharaonis dimer, 116 kDa Natronomonas pharaonis protein
Buffer: 1400 mM NaCl, 49.4 mM Na/Na-Pi, 1.0 mM EDTA, 0.05% DDM (D2O buffer), pH: 8
Experiment: SANS data collected at YuMO SANS TOF spectrometer, IBR-2, Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research on 2019 Feb 10
Molecular model of a sensor of two-component signaling system Scientific Reports 11(1) (2021)
Ryzhykau Y, Orekhov P, Rulev M, Vlasov A, Melnikov I, Volkov D, Nikolaev M, Zabelskii D, Murugova T, Chupin V, Rogachev A, Gruzinov A, Svergun D, Brennich M, Gushchin I, Soler-Lopez M, Bothe A, Büldt G, Leonard G, Engelhard M, Kuklin A, Gordeliy V
RgGuinier 9.9 nm
Dmax 36.5 nm

SASDKA7 – Bromodomain-containing protein 2, BRD2, tandem bromodomains (1 mg/ml)

UniProt ID: P25440 (71-455) Bromodomain-containing protein 2
Bromodomain-containing protein 2 experimental SAS data
Bromodomain-containing protein 2 Kratky plot
Sample: Bromodomain-containing protein 2 monomer, 43 kDa Homo sapiens protein
Buffer: 25 mM HEPES, 150 mM NaCl, and 2% glycerol, pH: 7.5
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2018 Sep 25
Multivalent nucleosome scaffolding by bromodomain and extraterminal domain tandem bromodomains. J Biol Chem :108289 (2025)
Olp MD, Bursch KL, Wynia-Smith SL, Nuñez R, Goetz CJ, Jackson V, Smith BC
RgGuinier 4.7 nm
Dmax 18.8 nm
VolumePorod 80 nm3

SASDKH8 – C-Terminal Cytoplasmatic Region of the Translocated Intimin Receptor

UniProt ID: B7UM99 (388-550) Translocated intimin receptor Tir
Translocated intimin receptor Tir experimental SAS data
Translocated intimin receptor Tir Kratky plot
Sample: Translocated intimin receptor Tir monomer, 18 kDa Escherichia coli O127:H6 … protein
Buffer: 20 mM Sodium Phosphate, 150 mM NaCl, 1 mM EDTA, pH: 6.5
Experiment: SAXS data collected at BM29, ESRF on 2018 Sep 15
The pathogen-encoded signalling receptor Tir exploits host-like intrinsic disorder for infection. Commun Biol 7(1):179 (2024)
Vieira MFM, Hernandez G, Zhong Q, Arbesú M, Veloso T, Gomes T, Martins ML, Monteiro H, Frazão C, Frankel G, Zanzoni A, Cordeiro TN
RgGuinier 3.8 nm
Dmax 12.8 nm
VolumePorod 46 nm3

SASDLA3 – Ubiquitin activating enzyme 5 with ubiquitin-fold modifier 1 (UBA5 5 mg/mL + UFM1 1.25 mg/ml)

UniProt ID: Q9GZZ9 (57-346) Ubiquitin-like modifier-activating enzyme 5

UniProt ID: P61960 (1-83) Ubiquitin fold modifer 1
Ubiquitin-like modifier-activating enzyme 5Ubiquitin fold modifer 1 experimental SAS data
SASREF model
Sample: Ubiquitin-like modifier-activating enzyme 5 dimer, 68 kDa Homo sapiens protein
Ubiquitin fold modifer 1 monomer, 9 kDa Homo sapiens protein
Buffer: 20 mM Tris, 50 mM NaCl, 2 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2020 Oct 29
Structure and dynamics of UBA5-UFM1 complex formation showing new insights in the UBA5 activation mechanism Journal of Structural Biology :107796 (2021)
Fuchs S, Kikhney A, Schubert R, Kaiser C, Liebau E, Svergun D, Betzel C, Perbandt M
RgGuinier 3.1 nm
Dmax 13.0 nm
VolumePorod 100 nm3

SASDLS3 – Interleukin 11 Mutein, complex with gp130 (domains 1-3) and IL-11Rα

UniProt ID: Q14626 (23-319) Interleukin-11 receptor subunit alpha

UniProt ID: None (None-None) Interleukin 11 Mutein

UniProt ID: P40189 (22-324) Interleukin-6 receptor subunit beta
Interleukin-11 receptor subunit alphaInterleukin 11 MuteinInterleukin-6 receptor subunit beta experimental SAS data
DAMMIN model
Sample: Interleukin-11 receptor subunit alpha monomer, 32 kDa Homo sapiens protein
Interleukin 11 Mutein monomer, 18 kDa Homo sapiens protein
Interleukin-6 receptor subunit beta monomer, 35 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM NaCl, 0.2% sodium azide, pH: 8.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2019 Jun 8
Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant Nature Communications 14(1) (2023)
Metcalfe R, Hanssen E, Fung K, Aizel K, Kosasih C, Zlatic C, Doughty L, Morton C, Leis A, Parker M, Gooley P, Putoczki T, Griffin M
RgGuinier 4.4 nm
Dmax 15.6 nm
VolumePorod 160 nm3

SASDL44 – Human Albumin (HNA2)

UniProt ID: P02768 (None-None) Albumin
Albumin experimental SAS data
Albumin Kratky plot
Sample: Albumin monomer, 69 kDa Homo sapiens protein
Buffer: 20 mM Tris, 150 mM KCl, 2% glycerol, pH: 7.4
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2020 Dec 1
Albumin in patients with liver disease shows an altered conformation. Commun Biol 4(1):731 (2021)
Paar M, Fengler VH, Rosenberg DJ, Krebs A, Stauber RE, Oettl K, Hammel M
RgGuinier 2.8 nm
Dmax 8.1 nm

SASDLY4 – Bacillus subtilis diadenylate cyclase CdaA: cytoplasmic domain

UniProt ID: Q45589 (97-273) Cyclic di-AMP synthase CdaA
Cyclic di-AMP synthase CdaA experimental SAS data
Cyclic di-AMP synthase CdaA Kratky plot
Sample: Cyclic di-AMP synthase CdaA dimer, 44 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 2.6 nm
Dmax 8.9 nm
VolumePorod 60 nm3