Structure, dynamics and roX2-lncRNA binding of tandem double-stranded RNA binding domains dsRBD1,2 of Drosophila helicase Maleless.

Ankush Jagtap PK, Müller M, Masiewicz P, von Bülow S, Hollmann NM, Chen PC, Simon B, Thomae AW, Becker PB, Hennig J, Nucleic Acids Res 47(8):4319-4333 (2019) Europe PMC

SASDF52 – dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE

Dosage compensation regulator
MWexperimental 15 kDa
MWexpected 29 kDa
VPorod 22 nm3
log I(s) 6.62×101 6.62×100 6.62×10-1 6.62×10-2
Dosage compensation regulator small angle scattering data  s, nm-1
ln I(s)
Dosage compensation regulator Guinier plot ln 6.63×101 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Dosage compensation regulator Kratky plot 1.104 0 3 sRg
p(r)
Dosage compensation regulator pair distance distribution function Rg: 3.3 nm 0 Dmax: 12.5 nm

Data validation


Fits and models


log I(s)
 s, nm-1
dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE Rg histogram Rg, nm
Dosage compensation regulator EOM/RANCH model
Dosage compensation regulator EOM/RANCH model
Dosage compensation regulator EOM/RANCH model
Dosage compensation regulator EOM/RANCH model

Synchrotron SAXS data from solutions of the dsRBD1 and dsRBD2 domains of Drosophila helicase dosage compensation regulator, MLE, in 20 mM NaPO4, 200 mM NaCl, 1 mM DTT, pH 6.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.09919 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). A solute concentration of 5 mg/ml was measured at 20°C. 10 successive 1 second frames were collected per sample (three replicates total). The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Construct contains an additional two amino acids (Gly-Ala) at the N-terminus as a remaining product the TEV-protease cleavage. The data displayed in this entry consists of merged data from three replicates of equal sample concentration (5.0 mg/ml). Thus, an effective total of 30 frames x 1s exposures is collated for this curve. The data were merged using Primus and datmerge of the ATSAS 2.8.4-1 package maintained by SBGrid.

Dosage compensation regulator (MLE)
Mol. type   Protein
Organism   Drosophila melanogaster
Olig. state   Monomer
Mon. MW   28.5 kDa
 
UniProt   P24785 (1-257)
Sequence   FASTA