| MWexperimental | 35 | kDa |
| MWexpected | 38 | kDa |
| VPorod | 50 | nm3 |
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log I(s)
4.97×10-2
4.97×10-3
4.97×10-4
4.97×10-5
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s, nm-1
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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 PMCSASDHD4 – Trimeric complex of myosin A with myosin light chain (MLC1, residues 66-210) and essential light chain (TgELC2) from Toxoplasma gondii
Myosin essential light chain 2Myosin light chain TgMLC1, residues 66-210
Myosin A
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Fits and models
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Synchrotron SAXS data from solutions of the trimeric complex between myosin A, the myosin light chain (MLC1, residues 66-210) and the essential light chain (TgELC2) from Toxoplasma gondii 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 85.00 μl sample at 15.5 mg/ml was injected at a 0.75 ml/min flow rate onto a GE Superdex 200 Increase 10/300 column at 20.2°C. 1800 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.
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