| MWexperimental | 53 | kDa |
| MWexpected | 49 | kDa |
| VPorod | 77 | nm3 |
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log I(s)
2.91×101
2.91×100
2.91×10-1
2.91×10-2
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s, nm-1
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Structural analysis of the SRP Alu domain from Plasmodium falciparum reveals a non-canonical open conformation.
Soni K, Kempf G, Manalastas-Cantos K, Hendricks A, Flemming D, Guizetti J, Simon B, Frischknecht F, Svergun DI, Wild K, Sinning I, Commun Biol 4(1):600 (2021) Europe PMCSASDK64 – Signal recognition particle SRP9/14 heterodimer in complex with the 5' domain of SRP Alu RNA from Plasmodium falciparum
Signal recognition particle 9Signal recognition particle 14
SRP Alu RNA 5' domain
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Fits and models
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Synchrotron SAXS data from solutions of the SRP9/14 heterodimer bound to the 5' domain of SRP Alu RNA in 20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, 1mM DTT, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a wavelength of λ = 0.099 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 200.00 μl sample at 2.4 mg/ml was injected at a 0.60 ml/min flow rate onto a GE Superdex 200 10/300 column at 20°C. 2500 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.
MONSA phase models are presented representing the fits to the data of the protein (top) and RNA (middle) components, and the final complex (bottom). |
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