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

SASDGV9 – Nucleolar RNA helicase 2 (DDX21) fragment 186-783

Nucleolar RNA helicase 2 fragment 186-783
MWexperimental 156 kDa
MWexpected 138 kDa
VPorod 297 nm3
log I(s) 7.88×101 7.88×100 7.88×10-1 7.88×10-2
Nucleolar RNA helicase 2 fragment 186-783 small angle scattering data  s, nm-1
ln I(s)
Nucleolar RNA helicase 2 fragment 186-783 Guinier plot ln 7.88×101 Rg: 4.8 nm 0 (4.8 nm)-2 s2
(sRg)2I(s)/I(0)
Nucleolar RNA helicase 2 fragment 186-783 Kratky plot 1.104 0 √3 sRg
p(r)
Nucleolar RNA helicase 2 fragment 186-783 pair distance distribution function Rg: 4.9 nm 0 Dmax: 17.6 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Nucleolar RNA helicase 2 fragment 186-783 DAMMIF model
Synchrotron SAXS data from solutions of Nucleolar RNA helicase 2 (DDX21) fragment 186-783 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. 3000 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 fragment 186-783 (DDx21 fragment 186-7)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Dimer
Mon. MW   68.8 kDa
 
UniProt   Q9NR30 (186-783)
Sequence   FASTA