A structural and biochemical comparison of Ribonuclease E homologues from pathogenic bacteria highlights species-specific properties.

Mardle CE, Shakespeare TJ, Butt LE, Goddard LR, Gowers DM, Atkins HS, Vincent HA, Callaghan AJ, Sci Rep 9(1):7952 (2019) Europe PMC

SASDE82 – Ribonuclease E from Burkholderia pseudomallei

Endoribonuclease E
MWexperimental 257 kDa
MWexpected 250 kDa
VPorod 437 nm3
log I(s) 2.61×10-2 2.61×10-3 2.61×10-4 2.61×10-5
Endoribonuclease E small angle scattering data  s, nm-1
ln I(s)
Endoribonuclease E Guinier plot ln 2.61×10-2 Rg: 4.8 nm 0 (4.8 nm)-2 s2
Endoribonuclease E Kratky plot 1.104 0 3 sRg
Endoribonuclease E pair distance distribution function Rg: 4.8 nm 0 Dmax: 14.9 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Ribonuclease E from Burkholderia pseudomallei in 10 mM DTT, 10 mM MgCl2, 0.5 M NaCl, 20 mM Tris, pH 8 were collected on the B21 beam line at the Diamond Light Source (Oxfordshire, UK) using a Pilatus 2M detector at a sample-detector distance of 4.0 m and at a wavelength of λ = 0.1 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 6.41 mg/ml was measured at 15°C. 640 successive 3 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.

Endoribonuclease E (RNase E)
Mol. type   Protein
Organism   Burkholderia pseudomallei
Olig. state   Tetramer
Mon. MW   62.6 kDa
UniProt   A0A0H3HN63 (1-532)
Sequence   FASTA