Probing the Architecture of a Multi-PDZ Domain Protein: Structure of PDZK1 in Solution.

Hajizadeh NR, Pieprzyk J, Skopintsev P, Flayhan A, Svergun DI, Löw C, Structure 26(11):1522-1533.e5 (2018) Europe PMC

SASDD85 – PDZK1 Domain 1-4

Uncharacterized protein C1orf159
MWI(0) 50 kDa
MWexpected 53 kDa
VPorod 120 nm3
log I(s) 4.30×10-2 4.30×10-3 4.30×10-4 4.30×10-5
Uncharacterized protein C1orf159 small angle scattering data  s, nm-1
ln I(s)
Uncharacterized protein C1orf159 Guinier plot ln 4.30×10-2 Rg: 3.9 nm 0 (3.9 nm)-2 s2
Uncharacterized protein C1orf159 Kratky plot 1.104 0 3 sRg
Uncharacterized protein C1orf159 pair distance distribution function Rg: 4.1 nm 0 Dmax: 15.0 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Uncharacterized protein C1orf159 GASBOR model

log I(s)
 s, nm-1
Uncharacterized protein C1orf159 MONSA model

log I(s)
 s, nm-1
Uncharacterized protein C1orf159 BUNCH model

Synchrotron SAXS data from solutions of PDZK1 Domain 1-4 in 20mM Hepes 150 NaCl 0.5 mM TCEP, pH 7.5 were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 2M detector at a sample-detector distance of 4 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.8 and 6.4 mg/ml were measured at 15°C. 30 successive 0.045 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Uncharacterized protein C1orf159
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   53.4 kDa
UniProt   Q5T2W7 (7-460)
Sequence   FASTA