Insights on the structural dynamics of Leishmania braziliensis Hsp90 molecular chaperone by small angle X-ray scattering.

Seraphim TV, Silva KP, Dores-Silva PR, Barbosa LR, Borges JC, Int J Biol Macromol 97:503-512 (2017) Europe PMC

SASDBD3 – Leishmania braziliensis heat shock protein 90 (Hsp90).

Leishmania braziliensis heat shock protein 90 (Hsp90)
MWexperimental 190 kDa
MWexpected 166 kDa
VPorod 380 nm3
log I(s) 3.70×10-1 3.70×10-2 3.70×10-3 3.70×10-4
Leishmania braziliensis heat shock protein 90 (Hsp90) small angle scattering data  s, nm-1
ln I(s)
Leishmania braziliensis heat shock protein 90 (Hsp90) Guinier plot ln 3.70×10-1 Rg: 5.3 nm 0 (5.3 nm)-2 s2
(sRg)2I(s)/I(0)
Leishmania braziliensis heat shock protein 90 (Hsp90) Kratky plot 1.104 0 √3 sRg
p(r)
Leishmania braziliensis heat shock protein 90 (Hsp90) pair distance distribution function Rg: 5.6 nm 0 Dmax: 21 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Leishmania braziliensis heat shock protein 90 (Hsp90) DAMMIN model
X-ray synchrotron radiation scattering data from solutions of full length Leishmania braziliensis heat shock protein 90 (Hsp90) in 25 mM Tris 100 mM NaCl, 1 mM 2-mercaptoethanol were collected on the SAXS2 Beamline camera on the storage ring Brazilian Synchrotron Light Laboratory (Campinas, Brazil) using a MAR Image Plate detector (s = 4π sin θ/λ, where 2θ is the scattering angle). The data were normalized to the intensity of the transmitted beam and radially averaged. The scattering of the solvent-blank was subtracted. The low angle data collected were obtained from a single concentration scattering curve.

Wavelength = UNKNOWN. Cell temperature = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN. Concentration = UNKNOWN

Leishmania braziliensis heat shock protein 90 (Hsp90) (L. brazilien.Hsp90)
Mol. type   Protein
Organism   Leishmania braziliensis
Olig. state   Dimer
Mon. MW   82.8 kDa
Sequence   FASTA