| MWexperimental | 36 | kDa |
| MWexpected | 36 | kDa |
| VPorod | 62 | nm3 |
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log I(s)
1.58×101
1.58×100
1.58×10-1
1.58×10-2
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s, nm-1
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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) DOISASDN73 – Microtubule affinity regulating kinase (isoform MARK2, wild type)
Serine/threonine-protein kinase MARK2|
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Fits and models
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Synchrotron SAXS
data from solutions of
Microtubule affinity regulating kinase (isoform MARK2, wild type)
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, 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 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
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