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All mutants were able to grow normally showing no difference with their respective controls.
All these mutants were able to accelerate the rate of insulin precipitation.
Interestingly, the mutants were able to grow and to produce macedocin at considerably higher concentrations of NaCl compared to the wild-type (up to 4.0% w/v).
Unexpectedly, this latter was able to inhibit a GH11 enzyme, but not GH12, whereas the mutants were able to modulate the inhibition capacity.
Finally, although individually expressed rhodopsin and arrestin-1 mutants were able to bind each other, a complex stable enough for crystallization was obtained only when both were expressed as a fusion protein.
The results indicated that Q140G and Q140A mutants were able to improve both activity and thermal stability of the enzyme while Q140N variant reduced the enzyme activity and destabilized it.
Scanning electron microscopy revealed that Δcph1, Δhst7 and Δcst20 mutants were able to filament and form structured biofilms displaying three-dimensional architecture similar to those formed by wild-type strains.
The Kim53Δpcm and Kim53ΔrpoS mutants were able to produce disease upon i.n.n
We observed that all septin mutants were able to infect corn plants, although they showed attenuated symptoms.
Not all mutants were able to be complemented and only strains that could be complemented were used for further studies.
None of the truncation mutants were able to support Shh palmitoylation above control levels (Fig. 1C, D).
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