Human AIP HSP90 complex

Robert Rambo.

SASDTK3 – Human aryl-hydrocarbon receptor-interacting protein (R9Q point mutant)

AH receptor-interacting protein (R9Q)
MWexperimental 32 kDa
MWexpected 39 kDa
VPorod 64 nm3
log I(s) 1.57×10-2 1.57×10-3 1.57×10-4 1.57×10-5
AH receptor-interacting protein (R9Q) small angle scattering data  s, nm-1
ln I(s)
AH receptor-interacting protein (R9Q) Guinier plot ln 1.57×10-2 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
AH receptor-interacting protein (R9Q) Kratky plot 1.104 0 √3 sRg
p(r)
AH receptor-interacting protein (R9Q) pair distance distribution function Rg: 3.0 nm 0 Dmax: 10.9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
AH receptor-interacting protein (R9Q) OTHER model
Synchrotron SAXS data from solutions of aryl-hydrocarbon receptor-interacting protein (R9Q point mutant) in 20 mM Tris-Cl pH 7.5, 100 mM NaCl, 1 mM DTT, 5% (v/v) glycerol, were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a sample-detector distance of 4 m and at a wavelength of λ = 0.12 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 45.00 μl sample at 10 mg/ml was injected at a 0.08 ml/min flow rate onto a Shodex KW400 series column at 25°C. 20 successive 3 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.

Final merged curve from SEC-SAXS used for fitting and modelling.

AH receptor-interacting protein (R9Q) ((HIS)6-AIP)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   39.0 kDa
 
UniProt   O00170 (2-330)
Sequence   FASTA