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

SASDTK9 – HIV-1 Envelope Glycoprotein SOSIP from the CH848 isolate at 40 °C

CH848.3.D0949.10.17chim.6R.DS.SOSIP.664 Env glycoprotein
MWexperimental 211 kDa
MWexpected 211 kDa
VPorod 764 nm3
log I(s) 1.17×101 1.17×100 1.17×10-1 1.17×10-2
CH848.3.D0949.10.17chim.6R.DS.SOSIP.664 Env glycoprotein small angle scattering data  s, nm-1
ln I(s)
CH848.3.D0949.10.17chim.6R.DS.SOSIP.664 Env glycoprotein Guinier plot ln 1.17×101 Rg: 5.3 nm 0 (5.3 nm)-2 s2
(sRg)2I(s)/I(0)
CH848.3.D0949.10.17chim.6R.DS.SOSIP.664 Env glycoprotein Kratky plot 1.104 0 √3 sRg
p(r)
CH848.3.D0949.10.17chim.6R.DS.SOSIP.664 Env glycoprotein pair distance distribution function Rg: 5.1 nm 0 Dmax: 15.3 nm

Data validation

There are no models related to this curve.

Static SAXS data from HIV-1 Envelope glycoprotein from the HIV-1 isolate CH848 at 40 °C in 15 mM HEPES, 150 mM NaCl, and pH 7.1 were collected 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). 25 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 < 0.25 nm-1.

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

CH848.3.D0949.10.17chim.6R.DS.SOSIP.664 Env glycoprotein (CH848 Env SOSIP)
Mol. type   Protein
Organism   HIV-1 group M
Olig. state   Trimer
Mon. MW   70.3 kDa
Sequence   FASTA