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To understand these effects, we have crystallised both mutants and solved their structures.
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Finally, we crystalized YfiR in complex with the YfiBL43P mutant and solved the structure at 1.78 Å resolution by molecular replacement using YfiR and YfiB as models.
Therefore, to obtain the structure of the holoenzyme, we engineered the F221/222A double mutant and solved its calcium-bound structure at 3.02 Å resolution.
Here, we undertook an analysis of the USP11 domain structure, investigated the impact of domain deletion mutants on the catalytic function, and solved the crystal structures of the human and rat USP11 N-terminal DUSP and UBL domains.
Both problems were timely detected and solved.
The best mutant effort em to a given population effort ep is found by calculating em where ∂w em,ep)/∂em = 0 (holding ep constant, and confirming ∂2w em,ep)/∂em2<0 and (∂2w em,ep)/∂em∂ep + ∂2w em,ep)/∂em2)<0 to satisfy conditions for mutant and population stability [10]), and solving the resulting equation for em = ep = e*.
In addition, the crystal structures of specific mutants were solved.
From a practical point of view, these two triple mutants have solved the original synthetic problem.
In particular, crystallographic structures in the frozen activated state of the wild type (WT) and bR mutants have been solved at the atomic resolution.
Now go forth and solve.
Represent and solve equations graphically.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com