SASBDB entries for UniProt ID:

SASDET3 – Armadillo repeat 7-11 from SAUL1

UniProt ID: Q9LM76 (382-801) U-box domain-containing protein 44

U-box domain-containing protein 44 experimental SAS data
SASREF MX model
Sample: U-box domain-containing protein 44 tetramer, 185 kDa Arabidopsis thaliana protein
Buffer: 50 mM Tris, 250 mM NaCl, pH: 9
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 2
Senescence-associated ubiquitin ligase 1 (SAUL1)
Haifa El Kilani, Al Kikhney
RgGuinier 4.5 nm
Dmax 17.4 nm
VolumePorod 245 nm3

SASDE26 – Albumin-insulin degludec 1:12 complex

UniProt ID: P02768 (25-609) Human Albumin (Recombumin(R) Elite, Albumedix Ltd.)

UniProt ID: P01308 (25-110) Insulin degludec(Tresiba(R), Novo Nordisk A/S)

Human Albumin (Recombumin(R) Elite, Albumedix Ltd.)Insulin degludec(Tresiba(R), Novo Nordisk A/S) experimental SAS data
SASREF CV model
Sample: Human Albumin (Recombumin(R) Elite, Albumedix Ltd.) monomer, 66 kDa protein
Insulin degludec(Tresiba(R), Novo Nordisk A/S) dodecamer, 73 kDa protein
Buffer: 25 mM Na2HPO4, 15.9 mM m-cresol, 15.9 mM phenol, 212.8 mM glycerol, 20 mM NaCl, pH: 7.6
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Jun 27
Solution structures of long-acting insulin analogues and their complexes with albumin. Acta Crystallogr D Struct Biol 75(Pt 3):272-282 (2019)
Ryberg LA, Sønderby P, Barrientos F, Bukrinski JT, Peters GHJ, Harris P
RgGuinier 3.8 nm
Dmax 13.4 nm
VolumePorod 179 nm3

SASDE89 – Interleukin-1 receptor accessory protein ectodomain with RII linker

UniProt ID: Q9NPH3 (21-348) Interleukin-1 receptor accessory protein ectodomains with RII linker

Interleukin-1 receptor accessory protein ectodomains with RII linker experimental SAS data
BILBOMD model
Sample: Interleukin-1 receptor accessory protein ectodomains with RII linker monomer, 41 kDa Homo sapiens protein
Buffer: 10mM HEPES, 150mM NaCl, 3% glycerol, pH: 7.2
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2017 Jul 24
Functional Relevance of Interleukin-1 Receptor Inter-domain Flexibility for Cytokine Binding and Signaling. Structure 27(8):1296-1307.e5 (2019)
Ge J, Remesh SG, Hammel M, Pan S, Mahan AD, Wang S, Wang X
RgGuinier 3.0 nm
Dmax 10.7 nm
VolumePorod 75 nm3

SASDF99 – Bovine serum albumin monomer - SEC-SAXS/WAXS coupled to multiangle laser and quasi-elastic light scattering (MALLS and QELS)

UniProt ID: P02769 (25-607) Bovine serum albumin

Bovine serum albumin experimental SAS data
GASBOR model
Sample: Bovine serum albumin monomer, 66 kDa Bos taurus protein
Buffer: 50 mM HEPES, 3% v/v glycerol,, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2017 Apr 23
Adding Size Exclusion Chromatography (SEC) and Light Scattering (LS) Devices to Obtain High-Quality Small Angle X-Ray Scattering (SAXS) Data Crystals 10(11):975 (2020)
Graewert M, Da Vela S, Gräwert T, Molodenskiy D, Blanchet C, Svergun D, Jeffries C
RgGuinier 2.8 nm
Dmax 8.3 nm
VolumePorod 95 nm3

SASDGC4 – Active dimer of truncated 6xHis Cytohesin-3 (Grp1, amino acids 14-390) with Inositol 1,3,4,5-tetrakis phosphate (parallel CORAL and MultiFoXS models)

UniProt ID: O08967 (14-390) Cytohesin-3

Cytohesin-3 experimental SAS data
CORAL model
Sample: Cytohesin-3 dimer, 90 kDa Mus musculus protein
Buffer: 20 mM Tris, 150 mM NaCl, 2 mM MgCl2, 0.1% 2-mercaptoethanol, 5% glycerol, 0.001 mM insitol 1,3,4,5-tetrakis phosphate, pH: 8
Experiment: SAXS data collected at BioCAT 18ID, Advanced Photon Source (APS), Argonne National Laboratory on 2013 Nov 15
Structural Organization and Dynamics of Homodimeric Cytohesin Family Arf GTPase Exchange Factors in Solution and on Membranes. Structure (2019)
Das S, Malaby AW, Nawrotek A, Zhang W, Zeghouf M, Maslen S, Skehel M, Chakravarthy S, Irving TC, Bilsel O, Cherfils J, Lambright DG
RgGuinier 5.1 nm
Dmax 25.7 nm
VolumePorod 168 nm3

SASDGA6 – Apoptosis-stimulating protein 2 of p53 (ASPP2(905-1128)) bound to the serine/threonine-protein phosphatase PP1-alpha catalytic subunit, extended

UniProt ID: P62136 (1-330) Serine/threonine-protein phosphatase PP1-alpha catalytic subunit

UniProt ID: Q13625 (905-1128) Apoptosis-stimulating of p53 protein 2

Serine/threonine-protein phosphatase PP1-alpha catalytic subunitApoptosis-stimulating of p53 protein 2 experimental SAS data
BILBOMD model
Sample: Serine/threonine-protein phosphatase PP1-alpha catalytic subunit monomer, 38 kDa Homo sapiens protein
Apoptosis-stimulating of p53 protein 2 monomer, 26 kDa Homo sapiens protein
Buffer: 25 mM Tris, 150 mM NaCl, 1 mM DTT, pH: 8
Experiment: SAXS data collected at 12.3.1 (SIBYLS), Advanced Light Source (ALS) on 2019 May 31
Flexible Tethering of ASPP Proteins Facilitates PP-1c Catalysis. Structure 27(10):1485-1496.e4 (2019)
Zhou Y, Millott R, Kim HJ, Peng S, Edwards RA, Skene-Arnold T, Hammel M, Lees-Miller SP, Tainer JA, Holmes CFB, Glover JNM
RgGuinier 3.3 nm
Dmax 11.7 nm
VolumePorod 172 nm3

SASDHZ7 – Escherichia coli RnlA (mRNA endoribonuclease toxin LS) - R318A single alanine mutant

UniProt ID: P52129 (2-357) mRNA endoribonuclease toxin LS - R318A mutant; N-terminal His-tagged

mRNA endoribonuclease toxin LS - R318A mutant; N-terminal His-tagged experimental SAS data
mRNA endoribonuclease toxin LS - R318A mutant; N-terminal His-tagged Kratky plot
Sample: MRNA endoribonuclease toxin LS - R318A mutant; N-terminal His-tagged dimer, 84 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 3.4 nm
Dmax 12.7 nm
VolumePorod 124 nm3

SASDJZ4 – DNA-dependent protein kinase/ X-ray repair cross-complementing protein 5 and 6 complex bound to DNA (DNA-PK monomer )

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

UniProt ID: P13010 (1-732) X-ray repair cross-complementing protein 5

UniProt ID: P78527 (10-4128) DNA-dependent protein kinase catalytic subunit

UniProt ID: None (None-None) dsDNA

X-ray repair cross-complementing protein 6X-ray repair cross-complementing protein 5DNA-dependent protein kinase catalytic subunitdsDNA 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 monomer, 83 kDa Homo sapiens protein
DNA-dependent protein kinase catalytic subunit monomer, 468 kDa Homo sapiens protein
DsDNA dimer, 21 kDa DNA
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 6.5 nm
Dmax 23.1 nm
VolumePorod 1090 nm3

SASDJW9 – Mammalian cell entry protein 4A (Mce4A36-400)

UniProt ID: I6YC99 (36-400) Mce-family protein Mce4A

UniProt ID: None (None-None) n-Dodecyl-β-D-Maltopyranoside

Mce-family protein Mce4An-Dodecyl-β-D-Maltopyranoside experimental SAS data
OTHER model
Sample: Mce-family protein Mce4A monomer, 44 kDa Mycobacterium tuberculosis (strain … protein
N-Dodecyl-β-D-Maltopyranoside 0, 102 kDa
Buffer: 50mM Tris, 500mM NaCl, 10% Glycerol, 5mM DDM, 1mM Beta-ME, pH: 8
Experiment: SAXS data collected at B21, Diamond Light Source on 2018 May 13
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 5.7 nm
Dmax 21.5 nm
VolumePorod 446 nm3

SASDK67 – SANS data for the sensory rhodopsin II / transducer complex in detergent at 4.0 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: 4000 mM NaCl, 100 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 Jan 25
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 8.9 nm
Dmax 39.0 nm