Structural analysis of monomeric retroviral reverse transcriptase in complex with an RNA/DNA hybrid.

Nowak E, Potrzebowski W, Konarev PV, Rausch JW, Bona MK, Svergun DI, Bujnicki JM, Le Grice SF, Nowotny M, Nucleic Acids Res 41(6):3874-87 (2013) Europe PMC


MWexperimental 76 kDa
MWexpected 75 kDa
VPorod 160 nm3
log I(s) 4.53×101 4.53×100 4.53×10-1 4.53×10-2
apo XMRV RT small angle scattering data  s, nm-1
ln I(s)
apo XMRV RT Guinier plot ln 4.53×101 Rg: 4 nm 0 (4 nm)-2 s2
apo XMRV RT Kratky plot 1.104 0 3 sRg
apo XMRV RT pair distance distribution function Rg: 4.0 nm 0 Dmax: 13.5 nm

Data validation

Fits and models

log I(s)
 s, nm-1
apo XMRV RT CRYSOL model

Synchrotron SAXS data from solutions of apo XMRV RT in 10 mM HEPES 100 mM KCl 5% Glycerol, pH 6.5 were collected on the EMBL X33 camera at the DORIS III storage ring (Hamburg, Germany) using a Pilatus 1M-W detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.15 nm , the range of momentum transfer 0.085 < s < 6.032 nm-1 was covered (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). at 10°C. Eight successive 15 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.

apo XMRV RT (XM)
Mol. type   Protein
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   75 kDa
Sequence   FASTA