SASBDB entries for UniProt ID:

SASDBM4 – The 1:1:9:1 crRNA:Cas6f:Cas7fv:Cas5fv CRISPR/Cas Type I-F long Cascade complex

UniProt ID: A4Y6G3 (1-183) Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family)

UniProt ID: A4Y6G2 (1-336) Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822)

UniProt ID: A4Y6G1 (1-315) Nonameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821)

UniProt ID: (None-None) long-crRNA: CRISPR/Cas Type I-F Cascade component
Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family)Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822)Nonameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821)long-crRNA: CRISPR/Cas Type I-F Cascade component experimental SAS data
DAMMIF model
Sample: Cas6f: CRISPR/Cas Type I-F Cascade component (CRISPR-associated protein, Csy4 family) monomer, 21 kDa Shewanella putrefaciens protein
Cas5fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1822) monomer, 38 kDa Shewanella putrefaciens protein
Nonameric Cas7fv: CRISPR/Cas Type I-F Cascade component (Uncharacterized protein, Sputcn32_1821) nonamer, 335 kDa Shewanella putrefaciens protein
Long-crRNA: CRISPR/Cas Type I-F Cascade component monomer, 25 kDa RNA
Buffer: 50 mM HEPES 150 mM NaCl 1mM DTT 1mM EDTA, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2016 Jan 30
Modulating the Cascade architecture of a minimal Type I-F CRISPR-Cas system. Nucleic Acids Res 44(12):5872-82 (2016)
Gleditzsch D, Müller-Esparza H, Pausch P, Sharma K, Dwarakanath S, Urlaub H, Bange G, Randau L
RgGuinier 6.5 nm
Dmax 21.6 nm

SASDBN4 – Callose synthase

UniProt ID: Q9ZT82 (570-1208) Callose synthase
Callose synthase experimental SAS data
CORAL model
Sample: Callose synthase octamer, 633 kDa Arabidopsis thaliana protein
Buffer: Tris, 50 mM NaCl, pH: 7.3
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 2
Structural Characterization of Cell Wall and Plasma Membrane Proteins of Arabidopsis thaliana University of Hamburg Dissertation 8022 (2016)
Haifa El Kilani
RgGuinier 8.0 nm
Dmax 30.0 nm
VolumePorod 1033 nm3

SASDBP4 – Neisseria meningitidis iron-regulated outer membrane lipoprotein FrpD

UniProt ID: Q08840 (43-271) Iron-regulated outer membrane lipoprotein FrpD
Iron-regulated outer membrane lipoprotein FrpD experimental SAS data
DAMMIN model
Sample: Iron-regulated outer membrane lipoprotein FrpD monomer, 27 kDa Neisseria meningitidis protein
Buffer: 10 mM Tris-HCl 150 mM NaCl 0.01% NaN3, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Oct 19
Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis. Sci Rep 7:40408 (2017)
Sviridova E, Rezacova P, Bondar A, Veverka V, Novak P, Schenk G, Svergun DI, Kuta Smatanova I, Bumba L
RgGuinier 2.2 nm
Dmax 6.5 nm
VolumePorod 41 nm3

SASDBQ4 – Neisseria meningitidis iron-regulated FrpD-FrpC lipoprotein/protein complex

UniProt ID: Q08840 (43-271) Iron-regulated outer membrane lipoprotein FrpD

UniProt ID: Q9JYV5 (1-414) Iron-regulated protein FrpC
Iron-regulated outer membrane lipoprotein FrpDIron-regulated protein FrpC experimental SAS data
DAMMIN model
Sample: Iron-regulated outer membrane lipoprotein FrpD monomer, 27 kDa Neisseria meningitidis protein
Iron-regulated protein FrpC monomer, 46 kDa Neisseria meningitidis protein
Buffer: 50 mM Tris-HCl 150 mM NaCl 0.01% NaN3, pH: 7.4
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 Oct 19
Structural basis of the interaction between the putative adhesion-involved and iron-regulated FrpD and FrpC proteins of Neisseria meningitidis. Sci Rep 7:40408 (2017)
Sviridova E, Rezacova P, Bondar A, Veverka V, Novak P, Schenk G, Svergun DI, Kuta Smatanova I, Bumba L
RgGuinier 3.7 nm
Dmax 13.5 nm
VolumePorod 123 nm3

SASDBS4 – Glutamate decarboxylase alpha (GadA) from E. coli, low salt

UniProt ID: P69908 (None-None) Glutamate decarboxylase alpha (GadA) from E. coli
Glutamate decarboxylase alpha (GadA) from E. coli experimental SAS data
SASREF MX model
Sample: Glutamate decarboxylase alpha (GadA) from E. coli monomer, 53 kDa Escherichia coli protein
Buffer: 50 mM Tris, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jul 29
X-Ray Solution Scattering Study of Four Escherichia coli Enzymes Involved in Stationary-Phase Metabolism. PLoS One 11(5):e0156105 (2016)
Dadinova LA, Shtykova EV, Konarev PV, Rodina EV, Snalina NE, Vorobyeva NN, Kurilova SA, Nazarova TI, Jeffries CM, Svergun DI
RgGuinier 4.4 nm
VolumePorod 450 nm3

SASDBT4 – Bovine serum albumin monomer (measured by SEC-SAXS)

UniProt ID: P02769 (25-607) Bovine serum albumin, monomer
Bovine serum albumin, monomer experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Bovine serum albumin, monomer monomer, 66 kDa Bos taurus protein
Buffer: 20 mM Tris 142 mM NaCl 5 % Glycerol 1mM DTT, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 22
Bovine Serum Albumin measured by SEC-SAXS
Martha Brennich
RgGuinier 2.7 nm
Dmax 8.2 nm
VolumePorod 118 nm3

SASDBU4 – Vaccinia primase D5 protein fragment containing the D5N and helicase domain

UniProt ID: P21010 (323-785) Primase D5 protein fragment containing the D5N and helicase domain
Primase D5 protein fragment containing the D5N and helicase domain experimental SAS data
DAMMIF model
Sample: Primase D5 protein fragment containing the D5N and helicase domain hexamer, 321 kDa Vaccinia virus protein
Buffer: 20 mM Tris 150 mM NaCL 5% glycerol 1mM DTT, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2014 Sep 26
Domain Organization of Vaccinia Virus Helicase-Primase D5. J Virol 90(9):4604-4613 (2016)
Hutin S, Ling WL, Round A, Effantin G, Reich S, Iseni F, Tarbouriech N, Schoehn G, Burmeister WP
RgGuinier 4.8 nm
Dmax 14.5 nm
VolumePorod 570 nm3

SASDBV4 – Vaccinia virus MVA F1L antiapoptotic Bcl-2 viral protein

UniProt ID: O57173 (1-202) MVA F1L antiapoptotic Bcl-2 viral protein
MVA F1L antiapoptotic Bcl-2 viral protein experimental SAS data
BUNCH model
Sample: MVA F1L antiapoptotic Bcl-2 viral protein dimer, 51 kDa Vaccinia virus protein
Buffer: 25 mM HEPES 150 mM NaCl 5 mM DTT, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2016 Apr 15
The N Terminus of the Vaccinia Virus Protein F1L Is an Intrinsically Unstructured Region That Is Not Involved in Apoptosis Regulation. J Biol Chem 291(28):14600-8 (2016)
Caria S, Marshall B, Burton RL, Campbell S, Pantaki-Eimany D, Hawkins CJ, Barry M, Kvansakul M
RgGuinier 3.4 nm
Dmax 16.2 nm
VolumePorod 74 nm3

SASDAL6 – Wild-type chalcone isomerase, ligand-free

UniProt ID: V9P0A9 (None-None) Bacterial chalcone isomerase
Bacterial chalcone isomerase experimental SAS data
Bacterial chalcone isomerase Kratky plot
Sample: Bacterial chalcone isomerase hexamer, 194 kDa Eubacterium ramulus protein
Buffer: 50 mM sodium phosphate, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 23
Structure and catalytic mechanism of the evolutionarily unique bacterial chalcone isomerase. Acta Crystallogr D Biol Crystallogr 71(Pt 4):907-17 (2015)
Thomsen M, Tuukkanen A, Dickerhoff J, Palm GJ, Kratzat H, Svergun DI, Weisz K, Bornscheuer UT, Hinrichs W
RgGuinier 4.0 nm
Dmax 13.0 nm
VolumePorod 320 nm3

SASDBW4 – Albumen gland precursor of ovorubin (lipoglycocarotenoprotein agPcOvo: an oligomeric protein)

UniProt ID: J7I2T6 (None-None) Perivitellin ovorubin-1

UniProt ID: J7HZ90 (None-None) Perivitellin ovorubin-2

UniProt ID: J7I5Z5 (None-None) Perivitellin ovorubin-3
Perivitellin ovorubin-1Perivitellin ovorubin-2Perivitellin ovorubin-3 experimental SAS data
DAMMIF model
Sample: Perivitellin ovorubin-1, 22 kDa Pomacea canaliculata protein
Perivitellin ovorubin-2, 24 kDa Pomacea canaliculata protein
Perivitellin ovorubin-3, 35 kDa Pomacea canaliculata protein
Buffer: 20 mM Tris-HCl, pH: 8.5
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2014 Jun 10
Apple Snail Perivitellin Precursor Properties Help Explain Predators' Feeding Behavior. Physiol Biochem Zool 90(4):461-470 (2017)
Cadierno MP, Dreon MS, Heras H
RgGuinier 4.3 nm
Dmax 14.9 nm
VolumePorod 526 nm3