Oligomerization process of Bcl-2 associated X protein revealed from intermediate structures in solution.

Shih O, Yeh YQ, Liao KF, Sung TC, Chiang YW, Jeng US, Phys Chem Chem Phys 19(11):7947-7954 (2017) Europe PMC

SASDC93 – Tetrameric apoptosis regulator BAX (Bcl-2 associated X)

Apoptosis regulator BAX (Bcl-2 associated X)
MWexperimental 86 kDa
MWexpected 85 kDa
VPorod 180 nm3
log I(s) 2.28×10-2 2.28×10-3 2.28×10-4 2.28×10-5
Apoptosis regulator BAX (Bcl-2 associated X) small angle scattering data  s, nm-1
ln I(s)
Apoptosis regulator BAX (Bcl-2 associated X) Guinier plot ln 2.29×10-2 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Apoptosis regulator BAX (Bcl-2 associated X) Kratky plot 1.104 0 √3 sRg
p(r)
Apoptosis regulator BAX (Bcl-2 associated X) pair distance distribution function Rg: 3.9 nm 0 Dmax: 12.0 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Apoptosis regulator BAX (Bcl-2 associated X) SASREF model
Synchrotron SAXS data from solutions of tetrameric apoptosis regulator BAX (Bcl-2 associated X) in 20mM sodium phosphate, 100mM NaCl, pH 8 were collected on the 23A beam line at the Taiwan Photon Source (NSRRC, Hsinchu, Taiwan) using a Pilatus 1M-F detector at a sample-detector distance of 3.2 m and at a wavelength of λ = 0.08266 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 15°C. Two successive 30 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted to obtain the SAXS profile displayed in this entry.

Storage temperature = UNKNOWN

Apoptosis regulator BAX (Bcl-2 associated X) (BAX)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Tetramer
Mon. MW   21.2 kDa
 
UniProt   Q07812 (1-192)
Sequence   FASTA