Hybrid Structural Analysis of the Arp2/3 Regulator Arpin Identifies Its Acidic Tail as a Primary Binding Epitope.

Fetics S, Thureau A, Campanacci V, Aumont-Nicaise M, Dang I, Gautreau A, Pérez J, Cherfils J, Structure 24(2):252-60 (2016) Europe PMC

SASDBU2 – Human Arpin (isoform 1)

Human Arpin
MWI(0) 27 kDa
MWexpected 25 kDa
VPorod 47 nm3
log I(s) 5.00×10-2 5.00×10-3 5.00×10-4 5.00×10-5
Human Arpin small angle scattering data  s, nm-1
ln I(s)
Human Arpin Guinier plot ln 5×10-2 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
Human Arpin Kratky plot 1.104 0 √3 sRg
p(r)
Human Arpin pair distance distribution function Rg: 2.8 nm 0 Dmax: 13.2 nm

Data validation

There are no models related to this curve.

X-ray synchrotron radiation scattering data from solutions of human arpin in 50mM HEPES, pH 7.5, 100mM NaCl, 1mM TCEP were collected at 15 C on the SWING Beamline, Synchrotron Soleil, Gif Sur Yvette, France using a PCCD170170 Aviex detector. These data are derived from size-exclusion chromatography-SAXS. Note: The original SAXS data where the momentum transfer s in inverse Angstroms (s = 4π sin θ/λ, where 2θ is the scattering angle) is included in the zip file associated with this entry.

Due to high concentration at the elution peak, the HPLC UV detector was saturated and the concentrations of the sample was consequently underestimated. In this case, the molecular mass is overestimated when assessing this parameter from I(0) and concentration.

Human Arpin (Human Arpin)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   24.9 kDa
 
UniProt   Q7Z6K5
Sequence   FASTA