The Human RNA Helicase DDX21 Presents a Dimerization Interface Necessary for Helicase Activity

Marcaida M, Kauzlaric A, Duperrex A, Sülzle J, Moncrieffe M, Adebajo D, Manley S, Trono D, Dal Peraro M, iScience 23(12):101811 (2020) DOI

SASDGY9 – Nucleolar RNA helicase 2 (DDX21) fragment 186-783 monomeric mutant

Nucleolar RNA helicase 2
MWexperimental 68 kDa
MWexpected 69 kDa
VPorod 111 nm3
log I(s) 4.46×101 4.46×100 4.46×10-1 4.46×10-2
Nucleolar RNA helicase 2 small angle scattering data  s, nm-1
ln I(s)
Nucleolar RNA helicase 2 Guinier plot ln 4.47×101 Rg: 4.1 nm 0 (4.1 nm)-2 s2
(sRg)2I(s)/I(0)
Nucleolar RNA helicase 2 Kratky plot 1.104 0 3 sRg
p(r)
Nucleolar RNA helicase 2 pair distance distribution function Rg: 4.4 nm 0 Dmax: 17.7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Nucleolar RNA helicase 2 (DDX21) fragment 186-783 monomeric mutant in 20 mM HEPES, 500 mM NaCl, 10 % Glycerol, 2 mM TCEP, pH 7.5 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and 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 100.00 μl sample at 10 mg/ml was injected at a 0.50 ml/min flow rate onto a GE Superose 6 Increase 10/300 column at 20°C. 2160 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.

Storage temperature = UNKNOWN

Nucleolar RNA helicase 2 (DDX21)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   69.2 kDa
 
UniProt   Q9NR30 (186-783)
Sequence   FASTA