Structural basis of self-assembly in the lipid-binding domain of mycobacterial polar growth factor Wag31

Choukate K, Chaudhuri B, IUCrJ 7(4):767-776 (2020) DOI

SASDHH4 – N-terminal domain of Wag31 from M. tuberculosis

Cell wall synthesis protein Wag31
MWexperimental 35 kDa
MWexpected 34 kDa
VPorod 52 nm3
log I(s) 7.83×100 7.83×10-1 7.83×10-2 7.83×10-3
Cell wall synthesis protein Wag31 small angle scattering data  s, nm-1
ln I(s)
Cell wall synthesis protein Wag31 Guinier plot ln 7.83×100 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
Cell wall synthesis protein Wag31 Kratky plot 1.104 0 3 sRg
p(r)
Cell wall synthesis protein Wag31 pair distance distribution function Rg: 2.9 nm 0 Dmax: 10 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the N-terminal domain of Wag3 in 20 mM Tris pH 7.5, 150 mM NaCl, 10% glycerol, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.8 m and at a wavelength of λ = 0.1 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 30.00 μl sample at 4.4 mg/ml was injected at a 1.00 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 20°C. 1500 successive 1 second frames were collected through the elution profile. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of an appropriate solvent blank solvent-blank was subtracted from the corresponding sample scattering measured through the SEC elution peak.

Storage temperature = UNKNOWN

Cell wall synthesis protein Wag31 (N-Wag31)
Mol. type   Protein
Organism   Mycobacterium tuberculosis
Olig. state   Tetramer
Mon. MW   8.6 kDa
 
UniProt   P9WMU1 (2-60)
Sequence   FASTA