Structural variability of EspG chaperones from mycobacterial ESX-1, ESX-3 and ESX-5 type VII secretion systems

Tuukkanen A, Freire D, Chan S, Arbing M, Reed R, Evans T, Zenkeviciutė G, Kim J, Kahng S, Sawaya M, Chaton C, Wilmanns M, Eisenberg D, Parret A, Korotkov K, (2018) DOI

SASDDU2 – EspG3 chaperone from Mycobacterium smegmatis (Sel-Met labelled)

EspG3 chaperone from Mycobacterium smegmatis
MWexperimental 24 kDa
MWexpected 32 kDa
log I(s) 1.93×10-3 1.93×10-4 1.93×10-5 1.93×10-6
EspG3 chaperone from Mycobacterium smegmatis small angle scattering data  s, nm-1
ln I(s)
EspG3 chaperone from Mycobacterium smegmatis Guinier plot ln 1.93×10-3 Rg: 2.6 nm 0 (2.6 nm)-2 s2
(sRg)2I(s)/I(0)
EspG3 chaperone from Mycobacterium smegmatis Kratky plot 1.104 0 √3 sRg
p(r)
EspG3 chaperone from Mycobacterium smegmatis pair distance distribution function Rg: 2.6 nm 0 Dmax: 9.2 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of EspG3 chaperone from Mycobacterium smegmatis (Sel-Met labelled) in 20 mM HEPES pH 7.5, 150 mM NaCl, pH 7.5 were collected on the EMBL P12 beam line at the PETRA III storage ring (DESY; Hamburg, Germany) using a Pilatus 2M detector at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 3.79 mg/ml was measured. 20 successive 0.050 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.

Cell temperature = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN

EspG3 chaperone from Mycobacterium smegmatis (EspG3Msm)
Mol. type   Protein
Organism   Mycobacterium smegmatis
Olig. state   Monomer
Mon. MW   31.8 kDa
 
UniProt   A0QQ45
Sequence   FASTA