Molecular mechanisms underlying the functions of biofilm forming protein of mycobacterium tuberculosis

farheen jahan.

SASDTS8 – rv0360c (conserved protein)

Conserved protein
MWI(0) 30 kDa
MWexpected 31 kDa
VPorod 40 nm3
log I(s) 6.32×105 6.32×104 6.32×103 6.32×102
Conserved protein small angle scattering data  s, nm-1
ln I(s)
Conserved protein Guinier plot ln 6.32×105 Rg: 1.9 nm 0 (1.9 nm)-2 s2
(sRg)2I(s)/I(0)
Conserved protein Kratky plot 1.104 0 √3 sRg
p(r)
Conserved protein pair distance distribution function Rg: 1.8 nm 0 Dmax: 4.4 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Conserved protein DAMFILT model
log I(s)
 s, nm-1
Conserved protein ALPHAFOLD model
SAXS data from solutions of rv0360c (conserved protein) in 50 mM Tris pH 7.5, 200 mM NaCl, 2% glycerol were collected using an Anton Paar SAXSpace instrument at the CSIR-Central Drug Research Institute (Lucknow, India) equipped with a Mythen2 R 1K detector at a sample-detector distance of 0.3 m and at a wavelength of λ = 0.154 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 6.00 mg/ml was measured at 16°C. Two successive 1800 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.

CAUTION: Dmax severely underestimated. CAUTION: The DAM model displayed in this entry did not generate the corresponding fit to the SAXS data, but represents the volume and bead-occupancy corrected shape derived from the spatial alignment of an unknown number of individual models.

Conserved protein (RVO360C)
Mol. type   Protein
Organism   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Olig. state   Dimer
Mon. MW   15.3 kDa
 
UniProt   O06310 (1-145)
Sequence   FASTA