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Both clusters displayed a similar decreasing trend in both time-course series.
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The remaining three clusters displayed a more complex pattern.
TIRF imaging showed that CaV1.2 clusters displayed a mean of 5.07 ± 0.15 (n = 10) discrete bleaching steps.
The two clusters displayed a large overlap zone (sympatry) and members of the two clusters also co-existed at sites 18, 19 and 21 (syntopy).
The double-integrated simulated spectra for the single iron-sulfur clusters display a ratio of 1∶1 indicating the presence of both clusters FeSI and FeSII in the same amount in the protein.
Using spatially-resolved spectroscopy of discrete regions, hardness ratio and temperature maps, we show that all three clusters display a complex temperature structure.
Clusters displaying a maximum of 53.3% identity with any known superfamily were considered a putative novel superfamily.
Due to the lack of number of cities, the confidence intervals from other clusters display a degree of overlaps.
All metabolites in the inter-class specific clusters display a pair distance of at least 7 in the reaction network.
Exceptions included isolate 5341 (MLVA cluster I) and NCIMB14265T (MLVA cluster II) that differed in PFGE type from other isolates in their clusters, displaying a single band difference.
Cluster formation could well be the initial process that allows selection and then stabilization of clusters displaying a strong contribution to fitness.
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