| MWexperimental | 58 | kDa |
| MWexpected | 56 | kDa |
| VPorod | 80 | nm3 |
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log I(s)
2.14×10-2
2.14×10-3
2.14×10-4
2.14×10-5
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s, nm-1
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Structural Insights into the Mechanism of a Nanobody That Stabilizes PAI-1 and Modulates Its Activity
Sillen M, Weeks S, Strelkov S, Declerck P, International Journal of Molecular Sciences 21(16):5859 (2020) DOISASDJW5 – Plasminogen activator inhibitor-1 (PAI-1) W175F bound to nanobody Nb93
Plasminogen activator inhibitor 1VHH-s-a93 (Ig module Nb93)
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Fits and models
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Synchrotron SAXS data from solutions of PAI-1 bound to Nb93 in 30 mM BIS-TRIS pH 5.5, 300 mM sodium chloride, 5% v/v glycerol were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.10332 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 50.00 μl sample at 13 mg/ml was injected at a 0.30 ml/min flow rate onto a Agilent Bio SEC-3, 300 Å column at 15°C. 480 successive 0.990 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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