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The density map of bound GTP (gray mesh) is contoured at 1.4σ above the means.
The density map of bound ATP (gray mesh) is contoured at 3σ above the means.
In (A ) and (B ) the Fo-Fc density (blue mesh) is contoured at 3σ for citrate and at 5σ for the two bound Na+ ions and the water molecule between them.
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The 2Fo-Fc electron density map, shown in blue mesh, was contoured at 1.2 σ.
Left: density map (gray mesh) of SAM is contoured at 1.4σ above the means.
The density map (gray mesh) of protein and bound ATP is contoured at 3σ above the means.
The density map (gray mesh) of protein and bound GTP is contoured at 3σ above the means.
The anomalous difference map for Se-Met is contoured at 4 σ as green meshes with Se-Met residues labelled.
(F ) The overall sigmaA-weighted 2| F O| − | F C| electron density map after refinement is contoured at 1.0 σ level as blue meshes for the complex of methylated Norrin Fz4CRD (stick model).
The initial density modified map from PHENIX AUTOSOL (Terwilliger, 2000, Terwilliger et al., 2009) calculated with experimental Se-Met SAD phases is contoured at 1.5 σ and shown as blue meshes.
Skin is contoured using my #FilmstarBronzeandGlow.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com