The vaccinia virus DNA polymerase structure provides insights into the mode of processivity factor binding.

Tarbouriech N, Ducournau C, Hutin S, Mas PJ, Man P, Forest E, Hart DJ, Peyrefitte CN, Burmeister WP, Iseni F
Nat Commun 8(1):1455 (2017 Nov 13)

PMID: 29129932 doi: 10.1038/s41467-017-01542-z

Submitted to SASBDB: 2017 Jun 27 Published in SASBDB: 2017 Nov 20

SASDCM5 – Vaccinia virus binary E9 polymerase / DNA complex 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 RgGuinier 3.5 nm Dmax 12.0 nm VolumePorod 210 nm3

SASDCN5 – Vaccinia virus DNA polymerase 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 RgGuinier 3.9 nm Dmax 12.0 nm VolumePorod 202 nm3

SASDCP5 – Vaccinia virus DNA polymerase processivity factor component A20 (C-terminal fragment) 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 RgGuinier 2.2 nm Dmax 7.4 nm VolumePorod 31 nm3