The Dimer Interface of the Membrane Type 1 Matrix Metalloproteinase Hemopexin Domain

Tochowicz A, Goettig P, Evans R, Visse R, Shitomi Y, Palmisano R, Ito N, Richter K, Maskos K, Franke D, Svergun D, Nagase H, Bode W, Itoh Y, Journal of Biological Chemistry 286(9):7587-7600 (2011) DOI

SASDNU2 – Homodimerization of a membrane type 1 matrix metalloproteinase (MT1-MMP)

Hemopexin
Hemopexin
MWexperimental 35 kDa
MWexpected 69 kDa
VPorod 48 nm3
log I(s) 1.93×102 1.93×101 1.93×100 1.93×10-1
Hemopexin Hemopexin small angle scattering data  s, nm-1
ln I(s)
Hemopexin Hemopexin Guinier plot ln 1.94×102 Rg: 2.3 nm 0 (2.3 nm)-2 s2
(sRg)2I(s)/I(0)
Hemopexin Hemopexin Kratky plot 1.104 0 3 sRg
p(r)
Hemopexin Hemopexin pair distance distribution function Rg: 2.4 nm 0 Dmax: 8 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Hemopexin Hemopexin CUSTOM IN-HOUSE model
Hemopexin Hemopexin CUSTOM IN-HOUSE model

log I(s)
 s, nm-1
Hemopexin Hemopexin CUSTOM IN-HOUSE model

log I(s)
 s, nm-1
Hemopexin Hemopexin CUSTOM IN-HOUSE model

Synchrotron SAXS data from solutions of Homodimerization of a membrane type 1 matrix metalloproteinase (MT1-MMP) in 50 mM HEPES, 150 mM NaCl, 10 mM CaCl2, 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 at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 1 and 2.3 mg/ml were measured . Two successive 60 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 concentrations were extrapolated to infinite dilution and merged with the higher concentration data to yield the final composite scattering curve.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN

Tags: X33
Hemopexin (Hpx14)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   23.0 kDa
 
UniProt   P02790
Sequence   FASTA
 
Hemopexin
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   23.0 kDa
 
UniProt   P02790
Sequence   FASTA