Structural role of essential light chains in the apicomplexan glideosome.

Pazicky S, Dhamotharan K, Kaszuba K, Mertens HDT, Gilberger T, Svergun D, Kosinski J, Weininger U, Löw C, Commun Biol 3(1):568 (2020) Europe PMC

SASDH64 – Plasmodium falciparum myosin essential light chain, N-terminal domain

Myosin essential light chain
MWI(0) 10 kDa
MWexpected 9 kDa
VPorod 12 nm3
log I(s) 7.10×10-3 7.10×10-4 7.10×10-5 7.10×10-6
Myosin essential light chain small angle scattering data  s, nm-1
ln I(s)
Myosin essential light chain Guinier plot ln 7.10×10-3 Rg: 1.4 nm 0 (1.4 nm)-2 s2
Myosin essential light chain Kratky plot 1.104 0 3 sRg
Myosin essential light chain pair distance distribution function Rg: 1.4 nm 0 Dmax: 4.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Myosin essential light chain PYMOL model

Synchrotron SAXS data from solutions of the Plasmodium falciparum myosin essential light chain N-terminal domain in 20 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP were collected on the EMBL P12 beam line at the PETRA III storage ring (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.75 mg/ml was measured at 20.1°C. 20 successive 0.045 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.

Myosin essential light chain (ELC)
Mol. type   Protein
Organism   Plasmodium falciparum
Olig. state   Monomer
Mon. MW   9.1 kDa
UniProt   Q8IJM4 (1-74)
Sequence   FASTA