SASBDB entries for UniProt ID:

SASDBX4 – Albumen gland precursor of perivitellin-2 (PcPV2)

UniProt ID: P0C8G7 (None-None) Perivitellin-2 31 kDa subunit

UniProt ID: P0C8G6 (None-None) Perivitellin-2 67 kDa subunit
Perivitellin-2 31 kDa subunitPerivitellin-2 67 kDa subunit experimental SAS data
DAMMIF model
Sample: Perivitellin-2 31 kDa subunit tetramer, 126 kDa Pomacea canaliculata protein
Perivitellin-2 67 kDa subunit tetramer, 250 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 4.8 nm
Dmax 17.0 nm
VolumePorod 294 nm3

SASDBY4 – Pentameric Nucleoplasmin-histone H2A/H2B complex

UniProt ID: Q6NUC7 (2-145) Nucleoplasmin core + A2

UniProt ID: Q6AZJ8 (2-130) Histone H2A (ΔAla127)

UniProt ID: P02281 (5-126) Histone H2B 1.1 (Ser33Thr)
Nucleoplasmin core + A2Histone H2A (ΔAla127)Histone H2B 1.1 (Ser33Thr) experimental SAS data
DAMFILT model
Sample: Nucleoplasmin core + A2 pentamer, 81 kDa Xenopus laevis protein
Histone H2A (ΔAla127) pentamer, 69 kDa Xenopus laevis protein
Histone H2B 1.1 (Ser33Thr) pentamer, 67 kDa Xenopus laevis protein
Buffer: 20 mM Tris. 150 mM NaCl, 1 mM EDTA, 5 mM DTT, pH: 8
Experiment: SAXS data collected at BL4-2, Stanford Synchrotron Radiation Lightsource (SSRL) on 2016 Jan 7
Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release. Nat Commun 8(1):2215 (2017)
Warren C, Matsui T, Karp JM, Onikubo T, Cahill S, Brenowitz M, Cowburn D, Girvin M, Shechter D
RgGuinier 4.4 nm
Dmax 14.0 nm
VolumePorod 402 nm3

SASDBZ4 – Tyrosine hydroxylase (Isoform 1, Homo sapiens)

UniProt ID: P07101 (1-497) Tyrosine hydroxylase, isoform 1
Tyrosine hydroxylase, isoform 1 experimental SAS data
BUNCH model
Sample: Tyrosine hydroxylase, isoform 1 tetramer, 222 kDa Homo sapiens protein
Buffer: 20 mM Na-HEPES 200 mM NaCl, pH: 7
Experiment: SAXS data collected at EMBL P12, PETRA III on 2015 Jun 14
Stable preparations of tyrosine hydroxylase provide the solution structure of the full-length enzyme. Sci Rep 6:30390 (2016)
Bezem MT, Baumann A, Skjærven L, Meyer R, Kursula P, Martinez A, Flydal MI
RgGuinier 4.7 nm
Dmax 20.0 nm
VolumePorod 520 nm3

SASDB25 – Cardiac myosin binding protein-C: domains C5-C6-C7

UniProt ID: Q14896 (641-964) Cardiac myosin binding protein-C: domains C5-C6-C7
Cardiac myosin binding protein-C: domains C5-C6-C7 experimental SAS data
Cardiac myosin binding protein-C: domains C5-C6-C7 Kratky plot
Sample: Cardiac myosin binding protein-C: domains C5-C6-C7 monomer, 36 kDa Homo sapiens protein
Buffer: 25 mM Tris-HCl, 250 mM NaCl, 2 mM TCEP, 0.02% sodium azide, pH: 7.5
Experiment: SAXS data collected at SAXS/WAXS, Australian Synchrotron on 2015 Apr 18
Clinically Linked Mutations in the Central Domains of Cardiac Myosin-Binding Protein C with Distinct Phenotypes Show Differential Structural Effects. Structure 24(1):105-115 (2016)
Nadvi NA, Michie KA, Kwan AH, Guss JM, Trewhella J
RgGuinier 3.8 nm
Dmax 14.1 nm
VolumePorod 55 nm3

SASDB35 – Staphylococcus aureus thiaminase II

UniProt ID: Q6GEY1 (None-None) Thiaminase type II enzyme
Thiaminase type II enzyme experimental SAS data
PDB (PROTEIN DATA BANK) model
Sample: Thiaminase type II enzyme tetramer, 107 kDa Staphylococcus aureus protein
Buffer: 100 mM Tris-HCl, pH: 7.5
Experiment: SAXS data collected at EMBL X33, DORIS III, DESY on 2011 May 11
Staphylococcus aureus thiaminase II: oligomerization warrants proteolytic protection against serine proteases. Acta Crystallogr D Biol Crystallogr 69(Pt 12):2320-9 (2013)
Begum A, Drebes J, Kikhney A, Müller IB, Perbandt M, Svergun D, Wrenger C, Betzel C
RgGuinier 3.4 nm
Dmax 11.0 nm
VolumePorod 168 nm3

SASDB45 – Trimeric periplasmic holdase chaperone protein Skp

UniProt ID: P0AEU7 (21-161) Periplasmic holdase chaperone protein Skp
Periplasmic holdase chaperone protein Skp experimental SAS data
Trimeric periplasmic holdase chaperone protein Skp Rg histogram
Sample: Periplasmic holdase chaperone protein Skp trimer, 47 kDa Escherichia coli protein
Buffer: 25 mM HEPES 150 mM NaCl 1 mM DTT, pH: 7.5
Experiment: SAXS data collected at EMBL P12, PETRA III on 2013 Sep 24
A Spring-Loaded Mechanism Governs the Clamp-like Dynamics of the Skp Chaperone. Structure 25(7):1079-1088.e3 (2017)
Holdbrook DA, Burmann BM, Huber RG, Petoukhov MV, Svergun DI, Hiller S, Bond PJ
RgGuinier 3.6 nm
Dmax 12.8 nm
VolumePorod 168 nm3

SASDB65 – Tyrosine-protein phosphatase (YopH)/putative yopH targeting protein (SycH) heterotrimeric complex

UniProt ID: I3NIC8 (1-141) SycH putative yopH targeting protein

UniProt ID: P08538 (1-129) Tyrosine-protein phosphatase YopH
SycH putative yopH targeting proteinTyrosine-protein phosphatase YopH experimental SAS data
CRYSOL model
Sample: SycH putative yopH targeting protein dimer, 32 kDa Yersinia pseudotuberculosis protein
Tyrosine-protein phosphatase YopH monomer, 14 kDa Yersinia pseudotuberculosis protein
Buffer: 50 mM HEPES 2mM TCEP, pH: 6.8
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 Aug 1
Global Disordering in Stereo-Specific Protein Association Biophysical Journal 112(3):33a (2017)
Gupta A, Reinartz I, Spilotros A, Jonna V, Hofer A, Svergun D, Schug A, Wolf-Watz M
RgGuinier 3.0 nm
Dmax 12.5 nm
VolumePorod 89 nm3

SASDB75 – Escherichia coli TraE protein: A VirB8 homolog from plasmid pKM101

UniProt ID: Q46703 (None-None) Escherichia coli TraE protein (VirB8 homolog)
Escherichia coli TraE protein (VirB8 homolog) experimental SAS data
GASBOR model
Sample: Escherichia coli TraE protein (VirB8 homolog) hexamer, 171 kDa Escherichia coli protein
Buffer: 50 mM sodium phosphate 300 mM NaCl 40 mM imidazole 0.15 % octyl glucose neopentyl glycol (OGNG), pH: 7.4
Experiment: SAXS data collected at G1, Cornell High Energy Synchrotron Source (CHESS) on 2016 Jun 2
VirB8 homolog TraE from plasmid pKM101 forms a hexameric ring structure and interacts with the VirB6 homolog TraD. Proc Natl Acad Sci U S A 115(23):5950-5955 (2018)
Casu B, Mary C, Sverzhinsky A, Fouillen A, Nanci A, Baron C
RgGuinier 4.4 nm
Dmax 13.7 nm
VolumePorod 360 nm3

SASDB85 – Self-processing module of iron-regulated protein FrpC (415-591)

UniProt ID: Q9JYV5 (415-591) Iron-regulated protein FrpC (amino acids 415-591)
Iron-regulated protein FrpC (amino acids 415-591) experimental SAS data
OTHER model
Sample: Iron-regulated protein FrpC (amino acids 415-591) monomer, 19 kDa Neisseria meningitidis protein
Buffer: 5 mM Tris 50 mM NaCl 10 mM CaCl2 0.1% NaN3, pH: 7.4
Experiment: SAXS data collected at Rigaku BioSAXS-1000, CEITEC on 2013 Oct 3
Self-processing module of Iron-regulated protein FrpC
Vojtěch Kubáň
RgGuinier 1.7 nm
Dmax 4.5 nm
VolumePorod 21 nm3

SASDB95 – Shigella outer membrane protein IcsA autotransporter

UniProt ID: Q7BCK4 (None-None) Outer membrane protein IcsA (53-758)
Outer membrane protein IcsA (53-758) experimental SAS data
DAMMIN model
Sample: Outer membrane protein IcsA (53-758) monomer, 72 kDa Shigella flexneri protein
Buffer: 50 mM Tris 150 mM NaCl 10 mM CaCl2 3% v/v glycerol, pH: 7.4
Experiment: SAXS data collected at EMBL P12, PETRA III on 2016 May 18
The Shigella Virulence Factor IcsA Relieves N-WASP Autoinhibition by Displacing the Verprolin Homology/Cofilin/Acidic (VCA) Domain. J Biol Chem 292(1):134-145 (2017)
Mauricio RP, Jeffries CM, Svergun DI, Deane JE
RgGuinier 3.7 nm
Dmax 13.2 nm
VolumePorod 103 nm3