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By virtue of this compensatory evolution, a well replicating and genetically stable C-strain mutant was produced that can be serologically differentiated from wildtype CSFV.
The F171D mutant was produced and indeed resulted fully active and three times more soluble than the WT, greatly facilitating its use in NMR screening experiments.
Recombinant CXCL10 (wildtype or mutant) was produced and purified as described before [28].
However, the circular dichroism spectra of the wild-type and mutant proteins had similar shapes, and the mutant was produced in vivo at the same level as the wild-type species [15].
As expected, the Cys184Ser mutant was produced with a yield comparable to that of the wild-type enzyme (18.5 versus 27 mg of pure protein obtained from a 1 litre culture, respectively) (Table 2).
Since each kind of mutant was produced at an identical rate, we assessed the disadvantage associated with losing specific nitrogen use abilities in different locations by considering the relative abundances of the different mutants (related approaches have a long history in population genetics, e.g. [26]).
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This observation prompted us to investigate whether the erg26 mutant was producing petites cells that have lost part or all of the mitochondrial genome at a high frequency.
Native-like MeuTXKα3 and its mutant were produced in Escherichia coli and their toxic function against Drosophila Shaker K+ channel and its mammalian counterparts (rKv1.1 rKv1.3) were assayed by two-electrode voltage clamp technique.
The rBos d 5 B and its H146P mutant were produced in a 1-liter scale.
The rBos d 5 B and its H146P mutant were produced in E. coli as soluble proteins to the periplasmic space and purified with chromatographic steps.
V. cholerae Endo III and the K120Q mutant were produced in JM101 strains.
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