Structural Variations in the Catalytic and Ubiquitin-associated Domains of Microtubule-associated Protein/Microtubule Affinity Regulating Kinase (MARK) 1 and MARK2

Marx A, Nugoor C, Müller J, Panneerselvam S, Timm T, Bilang M, Mylonas E, Svergun D, Mandelkow E, Mandelkow E, Journal of Biological Chemistry 281(37):27586-27599 (2006) DOI

SASDN63 – Microtubule affinity regulating kinase (isoform MARK2, T208E point mutant)

Serine/threonine-protein kinase MARK2
MWexperimental 37 kDa
MWexpected 36 kDa
VPorod 61 nm3
log I(s) 9.00×101 9.00×100 9.00×10-1 9.00×10-2
Serine/threonine-protein kinase MARK2 small angle scattering data  s, nm-1
ln I(s)
Serine/threonine-protein kinase MARK2 Guinier plot ln 9.01×101 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
Serine/threonine-protein kinase MARK2 Kratky plot 1.104 0 3 sRg
p(r)
Serine/threonine-protein kinase MARK2 pair distance distribution function Rg: 2.4 nm 0 Dmax: 8 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Serine/threonine-protein kinase MARK2 CUSTOM IN-HOUSE model

Synchrotron SAXS data from solutions of Microtubule affinity regulating kinase (isoform MARK2, T208E point mutant) in 0.1 M Bis-Tris, 0.2 M ammonium citrate, 1mM DTT, pH 6.5 were collected on the EMBL X33 beam line at the DORIS III 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 0.5 and 6 mg/ml were measured . Two successive 120 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.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN

Tags: X33
Serine/threonine-protein kinase MARK2 (MARK2 mutant)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   36.2 kDa
 
UniProt   Q7KZI7
Sequence   FASTA