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

SASDDR2 – EspG1 chaperone from Mycobacterium marinum

EspG1 from Mycobacterium marinum
MWexperimental 25 kDa
MWexpected 30 kDa
log I(s) 6.24×102 6.24×101 6.24×100 6.24×10-1
EspG1 from Mycobacterium marinum small angle scattering data  s, nm-1
ln I(s)
EspG1 from Mycobacterium marinum Guinier plot ln 6.24×102 Rg: 2.7 nm 0 (2.7 nm)-2 s2
(sRg)2I(s)/I(0)
EspG1 from Mycobacterium marinum Kratky plot 1.104 0 √3 sRg
p(r)
EspG1 from Mycobacterium marinum pair distance distribution function Rg: 2.9 nm 0 Dmax: 9.7 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of EspG1 chaperone from Mycobacterium marinum 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 1.00 mg/ml was measured at 20°C. 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.

Sample detector distance = UNKNOWN

EspG1 from Mycobacterium marinum (EspG1Mm)
Mol. type   Protein
Organism   Mycobacterium marinum
Olig. state   Monomer
Mon. MW   29.8 kDa
 
UniProt   B2HMS9
Sequence   FASTA