| MWexperimental | 127 | kDa |
| MWexpected | 126 | kDa |
| VPorod | 210 | nm3 |
|
log I(s)
8.79×101
8.79×100
8.79×10-1
8.79×10-2
|
s, nm-1
|
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) Europe PMCSASDCM5 – Vaccinia virus binary E9 polymerase / DNA complex
DNA polymerase E9 exo- mutantDNA oligomer template-primer hairpin
|
|
|
Fits and models
|
|
|
Synchrotron SAXS data from solutions of Binary E9 polymerase / DNA complex in 20 mM Tris HCl, 100 mM NaCl, 4 mM DTT, pH 7 were collected using size exclusion chromatography coupled SAXS (SEC-SAXS) on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.0992 nm (I(s) vs s, where s = 4πsinθ/λ and 2θ is the scattering angle). Data were collected at at 20°C during the course of elution (700 successive 1 second frames). The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the resulting subtracted curves were scaled and averaged.
Concentration min = UNKNOWN. Concentration max = UNKNOWN |
|
||||||||||||||||||||||||||||||||||||||||||||||||||||||