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Both the wild-type protein and K63A mutant were able to interact with CNOT7 in vitro (Fig. 2E and 2F), with respective dissociation constants (K d) of 3.25 × 107 M−1 ± 2.18 × 107 M−1 and 1.52 × 107 M−1 ± 6.04 × 106 M−1 as measured by isothermal calorimetry (ITC) (Fig. S4 and Table S3).

Similarly, wild-type p53 and the R337H mutant were able to suppress colony growth of SaOS-2 cells [9].

Indeed, during the clonal selection, only cells expressing high copy number of this severe mutant were able to undergo cell proliferation.

After 14 days of growth the wild type bacteria and XacFhaC mutant were able to form structured biofilm in rich medium, in contrast the ΔXacFhaB showed an amorphous conformation (Figure 4A).

Only the fully melanized ascospores from the mutant were able to germinate, whereas none of the not fully pigmented spores germinated.

Mutants unable to produce both signals (double mutant) were able to produce a biofilm, but unlike the wild type, their biofilms were much thinner, cells were more densely packed, and the typical biofilm architecture was lacking.

The G28A mutant was able to replicate as efficiently as the WT Jc1 in naive Huh-7.5 cells, indicating that this mutation does not affect HCV replication in the presence of normal miR-122 levels.

Notably, the MreC-R154D-T221R mutant was able to form a stable complex with PBP2 much like wild-type MreC, indicating that the three central residues in the PBP2 MreC interaction play the key stabilization role.

Over-expression of the previously isolated KS cDNA from pumpkin (Cu-curbita maxima) (CmKS) m the ga2 mutant was able to complement the mutant phenotype.

Subsequently we tested whether the MORN1.C4A palmitoylation site mutant was able to rescue the phenotype.

First, the F3/A mutant was able to stabilize the final aggregation stage of AChE586-599 (Figure 5A).