SASBDB entries for UniProt ID:

SASDCM5 – Vaccinia virus binary E9 polymerase / DNA complex

UniProt ID: P20509 (1-1006) DNA polymerase E9 exo- mutant

UniProt ID: (None-None) DNA oligomer template-primer hairpin
DNA polymerase E9 exo- mutantDNA oligomer template-primer hairpin experimental SAS data
PYMOL model
Sample: DNA polymerase E9 exo- mutant monomer, 117 kDa Vaccinia virus protein
DNA oligomer template-primer hairpin monomer, 9 kDa synthetic construct DNA
Buffer: 20 mM Tris HCl, 100 mM NaCl, 4 mM DTT, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2015 Mar 12
The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding. Nat Commun 8(1):1455 (2017)
Tarbouriech N, Ducournau C, Hutin S, Mas PJ, Man P, Forest E, Hart DJ, Peyrefitte CN, Burmeister WP, Iseni F
RgGuinier 3.5 nm
Dmax 12.0 nm
VolumePorod 210 nm3

SASDCN5 – Vaccinia virus DNA polymerase

UniProt ID: P20509 (1-1006) DNA polymerase E9
DNA polymerase E9 experimental SAS data
PYMOL model
Sample: DNA polymerase E9 monomer, 117 kDa Vaccinia virus protein
Buffer: 20 mM Tris HCl, 100 mM NaCl, 4 mM DTT, pH: 7
Experiment: SAXS data collected at BM29, ESRF on 2014 Nov 27
The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding. Nat Commun 8(1):1455 (2017)
Tarbouriech N, Ducournau C, Hutin S, Mas PJ, Man P, Forest E, Hart DJ, Peyrefitte CN, Burmeister WP, Iseni F
RgGuinier 3.9 nm
Dmax 12.0 nm
VolumePorod 202 nm3

SASDCP5 – Vaccinia virus DNA polymerase processivity factor component A20 (C-terminal fragment)

UniProt ID: P20995 (304-426) DNA polymerase processivity factor component A20 C-ter fragment
DNA polymerase processivity factor component A20 C-ter fragment experimental SAS data
DAMMIF model
Sample: DNA polymerase processivity factor component A20 C-ter fragment monomer, 17 kDa Vaccinia virus protein
Buffer: 25 mM Tris-HCl, 300 mM NaCl, pH: 7.5
Experiment: SAXS data collected at BM29, ESRF on 2016 Feb 5
The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding. Nat Commun 8(1):1455 (2017)
Tarbouriech N, Ducournau C, Hutin S, Mas PJ, Man P, Forest E, Hart DJ, Peyrefitte CN, Burmeister WP, Iseni F
RgGuinier 2.2 nm
Dmax 7.4 nm
VolumePorod 31 nm3

SASDCQ5 – SAXS on intact Doryteuthis squid lens 100% layer

UniProt ID: Q25367 (1-232) S-crystallin, Q25367_DOROP
S-crystallin, Q25367_DOROP experimental SAS data
DAMMIF model
Sample: S-crystallin, Q25367_DOROP dimer, 55 kDa Doryteuthis pealeii protein
Buffer: Tissue fluid, pH: 7
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 Jul 17
Eye patches: Protein assembly of index-gradient squid lenses. Science 357(6351):564-569 (2017)
Cai J, Townsend JP, Dodson TC, Heiney PA, Sweeney AM

SASDCR5 – SAXS on intact Doryteuthis squid lens 80% layer

UniProt ID: Q25367 (1-232) S-crystallin, Q25367_DOROP
S-crystallin, Q25367_DOROP experimental SAS data
DAMMIF model
Sample: S-crystallin, Q25367_DOROP dimer, 55 kDa Doryteuthis pealeii protein
Buffer: Tissue fluid, pH: 7
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 Jul 19
Eye patches: Protein assembly of index-gradient squid lenses. Science 357(6351):564-569 (2017)
Cai J, Townsend JP, Dodson TC, Heiney PA, Sweeney AM

SASDCS5 – SAXS on intact Doryteuthis squid lens 60% layer

UniProt ID: Q25367 (1-232) S-crystallin, Q25367_DOROP
S-crystallin, Q25367_DOROP experimental SAS data
DAMMIF model
Sample: S-crystallin, Q25367_DOROP dimer, 55 kDa Doryteuthis pealeii protein
Buffer: Tissue fluid, pH: 7
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 Jul 17
Eye patches: Protein assembly of index-gradient squid lenses. Science 357(6351):564-569 (2017)
Cai J, Townsend JP, Dodson TC, Heiney PA, Sweeney AM

SASDCT5 – SAXS on intact Doryteuthis squid lens 40% layer

UniProt ID: Q25367 (1-232) S-crystallin, Q25367_DOROP
S-crystallin, Q25367_DOROP experimental SAS data
DAMMIF model
Sample: S-crystallin, Q25367_DOROP dimer, 55 kDa Doryteuthis pealeii protein
Buffer: Tissue fluid, pH: 7
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2014 Jul 17
Eye patches: Protein assembly of index-gradient squid lenses. Science 357(6351):564-569 (2017)
Cai J, Townsend JP, Dodson TC, Heiney PA, Sweeney AM

SASDCU5 – SAXS dilution series on ground Doryteuthis squid lens 100% layer

UniProt ID: Q25367 (1-232) S-crystallin, Q25367_DOROP
S-crystallin, Q25367_DOROP experimental SAS data
S-crystallin, Q25367_DOROP Kratky plot
Sample: S-crystallin, Q25367_DOROP dimer, 55 kDa Doryteuthis pealeii protein
Buffer: PBS, phosphate buffered saline, pH: 7
Experiment: SAXS data collected at X9A, National Synchrotron Light Source (NSLS) on 2013 Nov 12
Eye patches: Protein assembly of index-gradient squid lenses. Science 357(6351):564-569 (2017)
Cai J, Townsend JP, Dodson TC, Heiney PA, Sweeney AM
RgGuinier 2.4 nm

SASDCV5 – Leishmania braziliensis p23A

UniProt ID: A4HNB5 (None-None) Uncharacterized protein
Uncharacterized protein experimental SAS data
DAMFILT model
Sample: Uncharacterized protein monomer, 22 kDa Leishmania braziliensis protein
Buffer: 25 mM Tris-HCl, 100 mM NaCl, 5 mM B-mercaptoethanol, pH: 8
Experiment: SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2012 Mar 26
Identification of two p23 co-chaperone isoforms in Leishmania braziliensis exhibiting similar structures and Hsp90 interaction properties despite divergent stabilities. FEBS J 282(2):388-406 (2015)
Batista FA, Almeida GS, Seraphim TV, Silva KP, Murta SM, Barbosa LR, Borges JC
RgGuinier 3.3 nm
Dmax 13.0 nm

SASDCW5 – Dimeric Sortilin at pH 7.4

UniProt ID: Q6PHU5 (None-None) Sortilin, also: Neurotensin-receptor 3
Sortilin, also: Neurotensin-receptor 3 experimental SAS data
DAMMIF model
Sample: Sortilin, also: Neurotensin-receptor 3 dimer, 153 kDa Mus musculus protein
Buffer: 25 mM HEPES pH 7.4, 150 mM NaCl, pH: 7.4
Experiment: SAXS data collected at BM29, ESRF on 2016 Apr 17
Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release. Nat Commun 8(1):1708 (2017)
Leloup N, Lössl P, Meijer DH, Brennich M, Heck AJR, Thies-Weesie DME, Janssen BJC
RgGuinier 3.9 nm
Dmax 11.0 nm
VolumePorod 275 nm3