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

SASDU42 – HIV-1 Envelope Glycoprotein SOSIP from a BG505 isolate containing T332N mutation at 25 °C

BG505SOSIP.664T332N Env glycoprotein
MWexperimental 213 kDa
MWexpected 213 kDa
VPorod 712 nm3
log I(s) 3.90×102 3.90×101 3.90×100 3.90×10-1
BG505SOSIP.664T332N Env glycoprotein small angle scattering data  s, nm-1
ln I(s)
BG505SOSIP.664T332N Env glycoprotein Guinier plot ln 3.91×102 Rg: 5.0 nm 0 (5.0 nm)-2 s2
(sRg)2I(s)/I(0)
BG505SOSIP.664T332N Env glycoprotein Kratky plot 1.104 0 √3 sRg
p(r)
BG505SOSIP.664T332N Env glycoprotein pair distance distribution function Rg: 4.9 nm 0 Dmax: 20.7 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of HIV-1 Envelope Glycoprotein SOSIP from a BG505 isolate containing T332N mutation 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.

BG505SOSIP.664T332N Env glycoprotein (BG505 Env SOSIP)
Mol. type   Protein
Organism   HIV-1 group M
Olig. state   Trimer
Mon. MW   71.1 kDa
Sequence   FASTA