The weak complex between RhoGAP protein ARHGAP22 and signal regulatory protein 14-3-3 has 1:2 stoichiometry and a single peptide binding mode.

Hu SH, Whitten AE, King GJ, Jones A, Rowland AF, James DE, Martin JL, PLoS One 7(8):e41731 (2012) Europe PMC

SASDH33 – Rho GTPase-activating protein 22

Rho GTPase-activating protein 22
MWI(0) 45 kDa
MWexpected 47 kDa
VPorod 88 nm3
log I(s) 4.11×10-2 4.11×10-3 4.11×10-4 4.11×10-5
Rho GTPase-activating protein 22 small angle scattering data  s, nm-1
ln I(s)
Rho GTPase-activating protein 22 Guinier plot ln 4.11×10-2 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Rho GTPase-activating protein 22 Kratky plot 1.104 0 √3 sRg
p(r)
Rho GTPase-activating protein 22 pair distance distribution function Rg: 3.3 nm 0 Dmax: 12 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Rho GTPase-activating protein 22 BUNCH model
X-ray synchrotron radiation scattering data from ARHGAP22 in 25 mM HEPES 150mM NaCl pH 7.5 were collected on the SAXS/WAXS beam line of the Australian Synchrotron (Melbourne, Australia) using a 2D Photon counting Pilatus 1M-W pixel detector (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle; λ=0.10332 nm). For both the sample and buffer, five successive 2 second frames were collected from ~80 ul of protein flowed past the beam, where the protein concentration was 1.25 mg/ml. The data were normalized to the intensity of the transmitted beam, place on an absolute scale against water, radially averaged and the scattering of the solvent-blank was subtracted. The models and corresponding fits are from a model optimised using BUNCH. Of note, the intensity error estimates are given as 2-standard errors, thus, the Chi values are a factor of two times lower in the log files than is actually the case.

Rho GTPase-activating protein 22 (ARHGAP22)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   47.2 kDa
 
UniProt   Q7Z5H3 (1-405)
Sequence   FASTA