Conserved Outer Tegument Component UL11 from Herpes Simplex Virus 1 Is an Intrinsically Disordered, RNA-Binding Protein.

Metrick CM, Koenigsberg AL, Heldwein EE, mBio 11(3) (2020) Europe PMC

SASDEX4 – Herpes simplex virus 1 tegument protein UL11

Cytoplasmic envelopment protein 3
MWexperimental 16 kDa
MWexpected 12 kDa
VPorod 30 nm3
log I(s) 4.77×10-3 4.77×10-4 4.77×10-5 4.77×10-6
Cytoplasmic envelopment protein 3 small angle scattering data  s, nm-1
ln I(s)
Cytoplasmic envelopment protein 3 Guinier plot ln 4.77×10-3 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
Cytoplasmic envelopment protein 3 Kratky plot 1.104 0 3 sRg
p(r)
Cytoplasmic envelopment protein 3 pair distance distribution function Rg: 2.6 nm 0 Dmax: 12 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Herpes simplex virus 1 tegument protein UL11 in 50 mM HEPES, 100 mM NaCl, 0.5 mM tris(2-carboxyethyl)phosphine (TCEP), pH 7.5, were collected on the G1 beam line at the Cornell High Energy Synchrotron Source (CHESS, Ithaca, NY, USA) using a Pilatus 200K detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.124612 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Size exclusion chromatography SAXS (SEC-SAXS) was performed at 25°C using a sample injection concentration of 18.00 mg/ml. 497 successive 2 second data frames were collected through the SEC elution profile. Data corresponding to the UL11 elution peak were normalized to the intensity of the transmitted beam and radially averaged. Normalized and reduced SAXS data corresponding to solvent-blank ('solute-free' buffer) from the SEC column were subtracted.

Cytoplasmic envelopment protein 3 (UL11)
Mol. type   Protein
Organism   Human alphaherpesvirus 1
Olig. state   Monomer
Mon. MW   11.6 kDa
 
UniProt   P04289 (1-96)
Sequence   FASTA