| MWexperimental | 44 | kDa |
| MWexpected | 44 | kDa |
| VPorod | 65 | nm3 |
|
log I(s)
2.90×10-2
2.90×10-3
2.90×10-4
2.90×10-5
|
s, nm-1
|
Low sequence identity but high structural and functional conservation: The case of Hsp70/Hsp90 organizing protein (Hop/Sti1) of Leishmania braziliensis.
Batista FAH, Seraphim TV, Santos CA, Gonzaga MR, Barbosa LRS, Ramos CHI, Borges JC, Arch Biochem Biophys 600:12-22 (2016) Europe PMCSASDB64 – Leishmania braziliensis stress-induced protein sti1 (LbHop TPR2A-TPR2B-DP2 construct)
Stress-induced protein sti1 (Hop TPR2A-TPR2B-DP2 construct)|
|
|
Fits and models
|
|
|
X-ray synchrotron radiation scattering data from solutions of stress-induced protein sti1 (Hop/Sti1), amino acids 171-547 (N-terminal truncation, Hop TPR2A-TPR2B-DP2 construct) in 25 mM Tris 100 mM NaCl, 1 mM EDTA, 1 mM β-mercaptoethanol were collected on the SAXS2 beam line at the Brazilian Synchrotron Light Laboratory (Campinas, Brazil) using a MAR Image Plate detector (s = 4π sin θ/λ, where 2θ is the scattering angle). Different solute concentrations in the range 1.40-8.50 mg/ml were measured. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the different curves were scaled for protein concentration. The low angle data collected were merged to yield the final composite scattering curve.
Wavelength = UNKNOWN. Cell temperature = UNKNOWN. Storage temperature = UNKNOWN. Sample detector distance = UNKNOWN. X-ray Exposure time = UNKNOWN. Number of frames = UNKNOWN |
|
|||||||||||||||||||||||||||