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

SASDDT2 – EspG3 chaperone from Mycobacterium tuberculosis

EspG3 chaperone from Mycobacterium tuberculosis
MWexperimental 23 kDa
MWexpected 34 kDa
log I(s) 5.82×102 5.82×101 5.82×100 5.82×10-1
EspG3 chaperone from Mycobacterium tuberculosis small angle scattering data  s, nm-1
ln I(s)
EspG3 chaperone from Mycobacterium tuberculosis Guinier plot ln 5.83×102 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
EspG3 chaperone from Mycobacterium tuberculosis Kratky plot 1.104 0 √3 sRg
p(r)
EspG3 chaperone from Mycobacterium tuberculosis pair distance distribution function Rg: 2.6 nm 0 Dmax: 9 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of EspG3 chaperone from Mycobacterium tuberculosis 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 1.10 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 tuberculosis (EspG3Mtb)
Mol. type   Protein
Organism   Mycobacterium tuberculosis
Olig. state   Other
Mon. MW   33.6 kDa
 
UniProt   P9WJC6
Sequence   FASTA