Domain Organization of Vaccinia Virus Helicase-Primase D5.

Hutin S, Ling WL, Round A, Effantin G, Reich S, Iseni F, Tarbouriech N, Schoehn G, Burmeister WP, J Virol 90(9):4604-4613 (2016) Europe PMC

SASDBU4 – Vaccinia primase D5 protein fragment containing the D5N and helicase domain

Primase D5 protein fragment containing the D5N and helicase domain
MWexperimental 345 kDa
MWexpected 321 kDa
VPorod 570 nm3
log I(s) 2.95×101 2.95×100 2.95×10-1 2.95×10-2
Primase D5 protein fragment containing the D5N and helicase domain small angle scattering data  s, nm-1
ln I(s)
Primase D5 protein fragment containing the D5N and helicase domain Guinier plot ln 2.95×101 Rg: 4.8 nm 0 (4.8 nm)-2 s2
(sRg)2I(s)/I(0)
Primase D5 protein fragment containing the D5N and helicase domain Kratky plot 1.104 0 √3 sRg
p(r)
Primase D5 protein fragment containing the D5N and helicase domain pair distance distribution function Rg: 4.7 nm 0 Dmax: 14.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Primase D5 protein fragment containing the D5N and helicase domain DAMMIF model
X-ray synchrotron radiation scattering data from solutions of the primase D5 protein fragment from Vaccinia virus containing the D5N and helicase domain in 20 mM Tris 150 mM NaCL, 5% glycerol, 1mM DTT pH 7 on the BM29 SAXS beam line at the ESRF (Grenoble, France) using a 2D Photon counting Pilatus 1M-W pixel detector (I(s) vs s; s = 4π sin θ/λ, where 2θ is the scattering angle and λ=0.1 nm). A solute concentration of 1.42 mg/ml was measured using 2000 successive 2 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 different curves were scaled and averaged.

Primase D5 protein fragment containing the D5N and helicase domain (Vaccinia D5 323-785)
Mol. type   Protein
Organism   Vaccinia virus
Olig. state   Hexamer
Mon. MW   53.5 kDa
 
UniProt   P21010 (323-785)
Sequence   FASTA