Molecular insights into the self‐assembly mechanism of dystrophia myotonica kinase

Garcia P, Ucurum Z, Bucher R, Svergun D, Huber T, Lustig A, Konarev P, Marino M, Mayans O, The FASEB Journal 20(8):1142-1151 (2006) DOI

SASDN93 – Dystrophiamyotonica kinase (DMPK)

Myotonin-protein kinase
MWexperimental 113 kDa
MWexpected 92 kDa
VPorod 173 nm3
log I(s) 1.45×104 1.45×103 1.45×102 1.45×101
Myotonin-protein kinase small angle scattering data  s, nm-1
ln I(s)
Myotonin-protein kinase Guinier plot ln 1.46×104 Rg: 3.9 nm 0 (3.9 nm)-2 s2
(sRg)2I(s)/I(0)
Myotonin-protein kinase Kratky plot 1.104 0 √3 sRg
p(r)
Myotonin-protein kinase pair distance distribution function Rg: 4.0 nm 0 Dmax: 13 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Myotonin-protein kinase PDB (PROTEIN DATA BANK) model
log I(s)
 s, nm-1
Myotonin-protein kinase DAMMIN model
log I(s)
 s, nm-1
Myotonin-protein kinase BUNCH model
Synchrotron SAXS data from solutions of Dystrophiamyotonica kinase (DMPK) in 50 mM TrisHCl 50mM NaCl, 2.5 mM-mercaptoethanol, pH 8 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 1.4 and 9.3 mg/ml were measured . One 300 second frame was 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
Myotonin-protein kinase
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   92.0 kDa
 
UniProt   Q09013
Sequence   FASTA
 
PDB ID   2ETR