The dynamic nature of the conserved tegument protein UL37 of herpesviruses.

Koenigsberg AL, Heldwein EE, J Biol Chem 293(41):15827-15839 (2018) Europe PMC

SASDEL4 – Residues 478-884 of pseudorabies virus tegument protein UL37

Tegument protein UL37
MWI(0) 44 kDa
MWexpected 43 kDa
log I(s) 8.10×10-3 8.10×10-4 8.10×10-5 8.10×10-6
Tegument protein UL37 small angle scattering data  s, nm-1
ln I(s)
Tegument protein UL37 Guinier plot ln 8.10×10-3 Rg: 3.9 nm 0 (3.9 nm)-2 s2
(sRg)2I(s)/I(0)
Tegument protein UL37 Kratky plot 1.104 0 √3 sRg
p(r)
Tegument protein UL37 pair distance distribution function Rg: 4.0 nm 0 Dmax: 12.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Tegument protein UL37 DAMMIN model
Synchrotron SAXS data, I(s) vs s (where s = 4πsinθ/λ, and 2θ is the scattering angle), were measured from the C-terminal half of the Pseudorabiesvirus tegument protein UL37 using continuous-flow size-exclusion chromatography SAXS (SEC-SAXS) on the G1 beam line at the Cornell High Energy Synchrotron Source (CHESS; Ithaca, NY, USA). Data were collected a using a Pilatus 200K detector at a sample-detector distance of 1.5 m and at a wavelength of λ = 0.125 nm. The SEC mobile phase consisted of 100 mM HEPES, 150 mM NaCl, 5% glycerol, 0.1 mM tris(2-carboxyethyl)phosphine (TCEP), pH 7.5, (4°C). The SAXS data measured from the SEC-elution (sample peak and buffer; 300 successive 2 s frames) were normalized to the intensity of the transmitted beam and radially averaged. The scattering of an appropriate solvent-blank was subtracted from the sample frames to produce the scaled and averaged data displayed in this entry.

SEC column = UNKNOWN. Sample injection volume = UNKNOWN. Flow rate = UNKNOWN

Tegument protein UL37 (PRV UL37C)
Mol. type   Protein
Organism   Suid alphaherpesvirus 1
Olig. state   Monomer
Mon. MW   43.5 kDa
 
UniProt   Q911W0 (478-884)
Sequence   FASTA