PICK1 is implicated in organelle motility in an Arp2/3 complex-independent manner.

Madasu Y, Yang C, Boczkowska M, Bethoney KA, Zwolak A, Rebowski G, Svitkina T, Dominguez R, Mol Biol Cell 26(7):1308-22 (2015) Europe PMC

SASDBL2 – MBP-PICK1 fusion

Maltose Binding Protein fused to Protein Interacting with C kinase 1
MWexperimental 172 kDa
MWexpected 174 kDa
VPorod 483 nm3
log I(s) 4.14×101 4.14×100 4.14×10-1 4.14×10-2
Maltose Binding Protein fused to Protein Interacting with C kinase 1 small angle scattering data  s, nm-1
ln I(s)
Maltose Binding Protein fused to Protein Interacting with C kinase 1 Guinier plot ln 4.14×101 Rg: 8.4 nm 0 (8.4 nm)-2 s2
(sRg)2I(s)/I(0)
Maltose Binding Protein fused to Protein Interacting with C kinase 1 Kratky plot 1.104 0 √3 sRg
p(r)
Maltose Binding Protein fused to Protein Interacting with C kinase 1 pair distance distribution function Rg: 8.7 nm 0 Dmax: 27.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Maltose Binding Protein fused to Protein Interacting with C kinase 1 CRYSOL model
Synchrotron SAXS data from solutions of MBP-PICK1 fusion in 50 mM Tris 300 mM NaCl 1 mM maltose 1 mM EGTA 2 mM DTT, pH 7.5 were collected on the G1 beam line at the Cornell High Energy Synchrotron Source (CHESS) storage ring (Ithaca, NY, USA) using a Finger Lakes CCD detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.5 and 7.5 mg/ml were measured at 4°C. 20 successive 40 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.

This dataset was collected at a concentration of 3.75 mg/ml.

Maltose Binding Protein fused to Protein Interacting with C kinase 1 (MBP-PICK1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   87.1 kDa
 
UniProt   Q9NRD5
Sequence   FASTA