Small Angle Scattering Biological Data Bank SASBDB

SASBDB entries for UniProt ID:

SASDC75 – Leishmania braziliensis SGT co-chaperone

UniProt ID: A4HIK6 (None-None) SGT protein

Sample:	SGT protein dimer, 92 kDa Leishmania braziliensis protein
Buffer:	20 mM Potassium Phosphate, 100 mM KCl, 10 mM EDTA, 1 mM B-mercaptoethanol, pH: 7.5
Experiment:	SAXS data collected at SAXS2 Beamline, Brazilian Synchrotron Light Laboratory on 2014 May 14

Structural and functional studies of the Leishmania braziliensis SGT co-chaperone indicate that it shares structural features with HIP and can interact with both Hsp90 and Hsp70 with similar affinities. Int J Biol Macromol 118(Pt A):693-706 (2018)
Coto ALS, Seraphim TV, Batista FAH, Dores-Silva PR, Barranco ABF, Teixeira FR, Gava LM, Borges JC

R_g^Guinier	4.5	nm
D_max	17.0	nm

SASDC85 – Leishmania braziliensis p23B

UniProt ID: A4HAD9 (None-None) Leishmania braziliensis p23 isoform B

Leishmania braziliensis p23 isoform B experimental SAS data

Sample:	Leishmania braziliensis p23 isoform B monomer, 23 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

R_g^Guinier	3.0	nm
D_max	13.0	nm

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

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

R_g^Guinier	3.5	nm
D_max	12.0	nm
Volume^Porod	210	nm³

SASDCN5 – Vaccinia virus DNA polymerase

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

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

R_g^Guinier	3.9	nm
D_max	12.0	nm
Volume^Porod	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

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

R_g^Guinier	2.2	nm
D_max	7.4	nm
Volume^Porod	31	nm³

SASDCQ5 – SAXS on intact Doryteuthis squid lens 100% layer