| MWexperimental | 114 | kDa |
| MWexpected | 181 | kDa |
| VPorod | 162 | nm3 |
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log I(s)
1.70×103
1.70×102
1.70×101
1.70×100
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s, nm-1
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Covalent inhibition of hAChE by organophosphates causes homodimer dissociation through long-range allosteric effects.
Blumenthal DK, Cheng X, Fajer M, Ho KY, Rohrer J, Gerlits O, Taylor P, Juneja P, Kovalevsky A, Radić Z, J Biol Chem :101007 (2021) Europe PMCSASDL82 – Human acetylcholinesterase, apo
acetylcholinesteraseacetylcholinesterase
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Fits and models
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Synchrotron SAXS
data from solutions of
Human acetylcholinesterase, apo
in
50 mM Tris/HCl, 100 mM NaCl, pH 7.4
were collected
on the
BL4-2 beam line
at the Stanford Synchrotron Radiation Lightsource (SSRL) storage ring
(Menlo Park, CA, USA)
using a Rayonix MX225-HE detector
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
One solute concentration of 2.00 mg/ml was measured
at 22°C.
10 successive
1 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.
Apo human acetylcholinesterase (UniProt ID P22303-1) with glycosylation at N265 and N464, starting at amino acid 32 and truncated at amino acid 578, plus a GPL sequence insert at the N-terminus. X-ray wavelength: UNKNOWN. |
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