| MWexperimental | 211 | kDa |
| MWexpected | 243 | kDa |
| VPorod | 500 | nm3 |
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log I(s)
1.34×102
1.34×101
1.34×100
1.34×10-1
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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 PMCSASDVP2 – Multimeric complex cosisted of Human Cathepsin G-Neutrophil elastase tetramers bound to S.aureus Protein Map Eap3 and Eap4 domains
Cathepsin GNeutrophil elastase
Eap34
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Fits and models
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Synchrotron SAXS
data from solutions of
Multimeric complex cosisted of Human Cathepsin G-Neutrophil elastase tetramers bound to S.aureus Protein Map Eap3 and Eap4 domains
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).
One solute concentration of 5.00 mg/ml was measured
at 20°C.
848 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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