A secreted bacterial protein protects bacteria from cationic antimicrobial peptides by entrapment in phase separated droplets

Ostan N, Cole G, Wang F, Reichheld S, Moore G, Pan C, Yu R, Lai C, Sharpe S, Lee H, Schryvers A, Moraes T, PNAS Nexus (2024) DOI

SASDTS7 – Bovine Lactoferrin

Lactoferrin
MWexperimental 86 kDa
MWexpected 75 kDa
VPorod 117 nm3
log I(s) 2.86×100 2.86×10-1 2.86×10-2 2.86×10-3
Lactoferrin small angle scattering data  s, nm-1
ln I(s)
Lactoferrin Guinier plot ln 2.86×100 Rg: 3.2 nm 0 (3.2 nm)-2 s2
(sRg)2I(s)/I(0)
Lactoferrin Kratky plot 1.104 0 3 sRg
p(r)
Lactoferrin pair distance distribution function Rg: 3.3 nm 0 Dmax: 11.5 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of lactoferrin in 20 mM HEPES, 150 mM NaCl, pH 7.4 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory (Lemont, IL, USA) using a Pilatus3 X 1M detector at a sample-detector distance of 3.6 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.00 mg/ml was measured at 22°C. 1800 successive 0.500 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.

Lactoferrin (Lf)
Mol. type   Protein
Organism   Bos taurus
Olig. state   Monomer
Mon. MW   75.2 kDa
 
UniProt   Q6LBN7 (1-681)
Sequence   FASTA