| MWexperimental | 111 | kDa |
| MWexpected | 117 | kDa |
| VPorod | 163 | nm3 |
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log I(s)
8.18×101
8.18×100
8.18×10-1
8.18×10-2
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s, nm-1
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S. aureus Eap is a polyvalent inhibitor of neutrophil serine proteases.
Mishra N, Gido CD, Herdendorf TJ, Hammel M, Hura GL, Fu ZQ, Geisbrecht BV, J Biol Chem 300(9):107627 (2024) Europe PMCSASDVM2 – Ternary complex consisted of Human Neutrophil elastase tetramer and S.aureus Protein map Eap4-domain-4 (Δ347-476Δ) (Complex: NE/Eap4/NE)
Neutrophil elastaseProtein map
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Fits and models
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Synchrotron SAXS
data from solutions of
Ternary complex consisted of Human Neutrophil elastase tetramer and S.aureus Protein map Eap4-domain-4 (Δ347-476Δ) (Complex: NE/Eap4/NE)
in
20 mM HEPES, 140 mM NaCl, pH 7.4
were collected
on the
12.3.1 (SIBYLS) beam line
at the Advanced Light Source (ALS) storage ring
(Berkeley, CA, USA)
using a Pilatus3 X 2M detector
at a sample-detector distance of 2.1 m and
at a wavelength of λ = 0.1127 nm
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 60.00 μl sample
at 5 mg/ml was injected at a 0.65 ml/min flow rate
onto a Shodex KW-803 column
at 20°C.
660 successive
2 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.
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