The solution structure and dynamics of the DH-PH module of PDZRhoGEF in isolation and in complex with nucleotide-free RhoA.

Cierpicki T, Bielnicki J, Zheng M, Gruszczyk J, Kasterka M, Petoukhov M, Zhang A, Fernandez EJ, Svergun DI, Derewenda U, Bushweller JH, Derewenda ZS, Protein Sci 18(10):2067-79 (2009) Europe PMC

SASDAH4 – DH-PH

DH-PH module of PDZRhoGEF
MWexperimental 40 kDa
MWexpected 41 kDa
VPorod 60 nm3
log I(s) 3.78×10-1 3.78×10-2 3.78×10-3 3.78×10-4
DH-PH module of PDZRhoGEF small angle scattering data  s, nm-1
ln I(s)
DH-PH module of PDZRhoGEF Guinier plot ln 3.78×10-1 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
DH-PH module of PDZRhoGEF Kratky plot 1.104 0 √3 sRg
p(r)
DH-PH module of PDZRhoGEF pair distance distribution function 0 Dmax: 9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
DH-PH module of PDZRhoGEF DAMMIN model
log I(s)
 s, nm-1
DH-PH module of PDZRhoGEF CRYSOL model
Synchrotron SAXS data from solutions of DH-PH in 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH 7.5 were collected on the EMBL X33 beam line at the DORIS III, DESY storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.9 and 4.7 mg/ml were measured at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Wavelength = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN

Tags: X33
DH-PH module of PDZRhoGEF (DH-PH)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   41 kDa
Sequence   FASTA