Microsecond dynamics control the HIV-1 Envelope conformation.

Bennett AL Edwards R, Kosheleva I, Saunders C, Bililign Y, Williams A, Bubphamala P, Manosouri K, Anasti K, Saunders KO, Alam SM, Haynes BF, Acharya P, Henderson R, Sci Adv 10(5):eadj0396 (2024) Europe PMC

SASDTY9 – HIV-1 Envelope Glycoprotein SOSIP from a transmitted founder virus of the CH505 isolate at 25 °C

CH505TFchim.6R.SOSIP.664 Env glycoprotein
MWexperimental 210 kDa
MWexpected 217 kDa
VPorod 731 nm3
log I(s) 4.10×102 4.10×101 4.10×100 4.10×10-1
CH505TFchim.6R.SOSIP.664 Env glycoprotein small angle scattering data  s, nm-1
ln I(s)
CH505TFchim.6R.SOSIP.664 Env glycoprotein Guinier plot ln 4.10×102 Rg: 5.3 nm 0 (5.3 nm)-2 s2
(sRg)2I(s)/I(0)
CH505TFchim.6R.SOSIP.664 Env glycoprotein Kratky plot 1.104 0 √3 sRg
p(r)
CH505TFchim.6R.SOSIP.664 Env glycoprotein pair distance distribution function Rg: 5.3 nm 0 Dmax: 16.1 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of HIV-1 Envelope Glycoprotein SOSIP from a transmitted founder virus of the CH505 isolate in 15 mM HEPES, 150 mM NaCl, pH 7.1 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS; Berkeley, CA, USA) using a MAR 165 CCD detector at a wavelength of λ = 0.1 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.00 mg/ml was measured at 25°C for a total exposure time of 10 s. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Data reduction was performed in the SIBYLS Beamline reduction software. Data analysis was performed using the ATSAS package.

CH505TFchim.6R.SOSIP.664 Env glycoprotein (CH505TF SOSIP Env)
Mol. type   Protein
Organism   HIV-1 group M
Olig. state   Trimer
Mon. MW   72.5 kDa
Sequence   FASTA