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

SASDH74 – Plasmodium falciparum myosin essential light chain, full-length

Myosin essential light chain
MWexperimental 16 kDa
MWexpected 16 kDa
VPorod 23 nm3
log I(s) 6.59×10-3 6.59×10-4 6.59×10-5 6.59×10-6
Myosin essential light chain small angle scattering data  s, nm-1
ln I(s)
Myosin essential light chain Guinier plot ln 6.60×10-3 Rg: 2.7 nm 0 (2.7 nm)-2 s2
Myosin essential light chain Kratky plot 1.104 0 3 sRg
Myosin essential light chain pair distance distribution function Rg: 2.8 nm 0 Dmax: 9.5 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of full-length Plasmodium falciparum myosin essential light chain 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). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A sample at 10 mg/ml was injected at a 0.40 ml/min flow rate onto a GE Superdex 200 Increase 5/150 column at 10°C. 900 successive 0.995 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.

Sample injection volume = UNKNOWN

Myosin essential light chain (ELC)
Mol. type   Protein
Organism   Plasmodium falciparum
Olig. state   Monomer
Mon. MW   15.8 kDa
UniProt   Q8IJM4 (1-134)
Sequence   FASTA