Human myelin protein P2: from crystallography to time-lapse membrane imaging and neuropathy-associated variants.

Uusitalo M, Klenow MB, Laulumaa S, Blakeley MP, Simonsen AC, Ruskamo S, Kursula P, FEBS J (2021) Europe PMC

SASDLD5 – CMT mutant V115A of human myelin protein P2

Human P2 V115A mutant
MWexperimental 14 kDa
MWexpected 15 kDa
VPorod 17 nm3
log I(s) 3.15×10-2 3.15×10-3 3.15×10-4 3.15×10-5
Human P2 V115A mutant small angle scattering data  s, nm-1
ln I(s)
Human P2 V115A mutant Guinier plot ln 3.15×10-2 Rg: 1.5 nm 0 (1.5 nm)-2 s2
Human P2 V115A mutant Kratky plot 1.104 0 3 sRg
Human P2 V115A mutant pair distance distribution function Rg: 1.4 nm 0 Dmax: 4.0 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Human P2 V115A mutant DAMMIN model

Synchrotron SAXS data from solutions of CMT mutant V115A of human myelin protein P2 in 20 mM HEPES, 300 mM NaCl, 1 mM DTT, pH 7.5 were collected on the B21 beam line at the Diamond Light Source (Didcot, UK) using a Eiger 4M detector at a wavelength of λ = 0.095 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A sample at 8.9 mg/ml was injected at a 0.075 ml/min flow rate onto a GE Superdex 200 Increase 3.2/300 column at 20°C. 30 successive 3 second frames were collected through the SEC peak. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Human P2 V115A mutant
Mol. type   Protein
Olig. state   Monomer
Mon. MW   14.9 kDa
Sequence   FASTA