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 PMC

SASDK44 – The 5' domain of SRP Alu RNA from Plasmodium falciparum

SRP Alu RNA 5' domain

MW^experimental	27	kDa
MW^expected	24	kDa
V^Porod	38	nm³

log I(s) 9.42×10¹ 9.42×10⁰ 9.42×10^-1 9.42×10^-2

SRP Alu RNA 5' domain small angle scattering data

s, nm^-1

Log plot Log-Log plot

ln I(s)

ln 9.42×10¹ R_g: 3.3 nm 0 (3.3 nm)^-2 s²

(sR_g)²I(s)/I(0)

1.104 0 √3 sR_g

p(r)	R_g: 3.4 nm 0 D_max: 11.5 nm

Data validation

Experimental data range

p(r) fit to data

Metric

Value

s_min D_max / π

0.7

N_Shannon

Worse

Better

Metric

Value

p_cormap

χ²

0.002
1.227

Worse

Better

Fits and models

log I(s)	s, nm^-1
+3 Δ/σ -3	s, nm^-1

Synchrotron SAXS data from solutions of the 5' domain of SRP Alu RNA in 20 mM HEPES pH 7.5, 150 mM NaCl, 10 mM MgCl2, 10 mM KCl, 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). One solute concentration of 0.45 mg/ml was measured at 20°C. 20 successive 0.500 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.

Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

SRP Alu RNA 5' domain
Mol. type		RNA
Organism		Plasmodium falciparum
Olig. state		Monomer
Mon. MW		24.4 kDa
Sequence		FASTA