Molecular Insights on the Assembling of ParB1 and ParB1- parS1 Partition Complex

Anu A, Lata S, Chaudhuri B, ACS Bio & Med Chem Au (2026) DOI

SASDVD3 – Full-length dimeric Probable chromosome-partitioning protein ParB-peak

Probable chromosome-partitioning protein ParB
MWexperimental 60 kDa
MWexpected 68 kDa
VPorod 130 nm3
log I(s) 2.24×101 2.24×100 2.24×10-1 2.24×10-2
Probable chromosome-partitioning protein ParB small angle scattering data  s, nm-1
ln I(s)
Probable chromosome-partitioning protein ParB Guinier plot ln 2.25×101 Rg: 4.2 nm 0 (4.2 nm)-2 s2
(sRg)2I(s)/I(0)
Probable chromosome-partitioning protein ParB Kratky plot 1.104 0 3 sRg
p(r)
Probable chromosome-partitioning protein ParB pair distance distribution function Rg: 4.3 nm 0 Dmax: 16.7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Full-length dimeric Probable chromosome-partitioning protein ParB-peak in 20 mM Tris,100 mM NaCl,2% glycerol,1 mM EDTA,2 mM DTT,5 mM MgCl2, 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 2.8 m and at a wavelength of λ = 0.0999 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 0.07 ml/min flow rate onto a GE Superdex 200 Increase 3.2/300 column at 20°C. 960 successive 2 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.

SEC-SAXS experiments were performed at beamline BM29 at ESRF.

Probable chromosome-partitioning protein ParB (vcParB1)
Mol. type   Protein
Organism   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Olig. state   Dimer
Mon. MW   34.1 kDa
 
UniProt   Q9KNG7 (2-293)
Sequence   FASTA