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

SASDT59 – HIV-1 Envelope Glycoprotein SOSIP from a transmitted founder virus of the CH505 isolate at 50 °C

CH505TFchim.6R.SOSIP.664 Env glycoprotein
MWexperimental 340 kDa
MWexpected 217 kDa
VPorod 699 nm3
log I(s) 1.41×101 1.41×100 1.41×10-1 1.41×10-2
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 1.41×101 Rg: 4.6 nm 0 (4.6 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: 5.2 nm 0 Dmax: 15.6 nm

Data validation

There are no models related to this curve.

Static SAXS data from HIV-1 Envelope glycoprotein from the transmitted founder virus HIV-1 isolate CH505 collected 50 °C in 15 mM HEPES, 150 mM NaCl, pH 7.1 were on the 14-ID BioCARS Beamline at the Advanced Photon Source (APS) storage ring (Argonne National Laboratory) using a Rayonix MX340-HS X-ray detector using pink X-ray beam with photon energy 12 keV and bandpass of 300 eV (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). 50 images were collected with 24 bunches with 197 pulses at 3.6 μs/pulse exposure time per image. The data were normalized to the isosbestic point of water and radially averaged; the scattering of the HEPES solvent-blank was subtracted. Data reduction was performed in the BioCARS 14-ID Beamline reduction software and masked for s < 0.2 nm-1.

Data analysis was performed using https://gitlab.oit.duke.edu/tr_t-jump_saxs/y22-23 v1.0.0

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