Structural insights into the dynamics and function of the C-terminus of the E. coli RNA chaperone Hfq.

Beich-Frandsen M, Vecerek B, Konarev PV, Sjöblom B, Kloiber K, Hämmerle H, Rajkowitsch L, Miles AJ, Kontaxis G, Wallace BA, Svergun DI, Konrat R, Bläsi U, Djinovic-Carugo K, Nucleic Acids Res 39(11):4900-15 (2011) Europe PMC

SASDAG5 – RNA shaperone Hfq

RNA chaperone Hfq
MWexperimental 67 kDa
MWexpected 67 kDa
VPorod 110 nm3
log I(s) 1.30×102 1.30×101 1.30×100 1.30×10-1
RNA chaperone Hfq small angle scattering data  s, nm-1
ln I(s)
RNA chaperone Hfq Guinier plot ln 1.30×102 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
RNA chaperone Hfq Kratky plot 1.104 0 3 sRg
p(r)
RNA chaperone Hfq pair distance distribution function Rg: 3.2 nm 0 Dmax: 11.2 nm

Data validation


Fits and models


log I(s)
 s, nm-1
RNA chaperone Hfq DAMMIN model

log I(s)
 s, nm-1
RNA chaperone Hfq BUNCH model

Synchrotron SAXS data from solutions of RNA shaperone Hfq in 50 mM Tris-HCL 150 mM NaCl 1.0 mM DTT, pH 7.5 were collected on the EMBL X33 beam line at the DORIS III storage ring (Hamburg, Germany) using a MAR 345 Image Plate detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 2.3 and 18.5 mg/ml were measured at 37°C. Two successive 120 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

Tags: X33
RNA chaperone Hfq (Hfq)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Hexamer
Mon. MW   11.2 kDa
Sequence   FASTA