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This Week in Nature: May 5, 2011

In a paper published online in advance in Nature Genetics this week, a team led by investigators at Baylor College of Medicine reports its quantification of mRNA copy-number statistics from 20 E. coli promoters — via single-molecule fluorescence in situ hybridization — for the purpose of characterizing the general properties of transcriptional time series in the bacterium. The team says it found that "the degree of burstiness is correlated with gene expression level but is largely independent of other parameters of gene regulation." The authors also report their estimation of the mutual information transmitted between an outside stimulus and intracellular mRNA levels.

Over in this week's Nature, the University of Washington's Frank DiMaio and his colleagues show that by "combining algorithms for protein structure modeling with those developed for crystallographic structure determination," they could rapidly determine protein structure without experimental phase information. "We estimate that the new method should allow rapid structure determination ... for over half the cases where current methods fail," given they satisfy three requirements: diffraction data of greater than 3.2Å resolution, four or fewer copies in the asymmetric unit, and the established availability of structures for homologous proteins that shared greater than 20 percent sequence identity with the protein of interest, DiMaio et al. report.

In a Nature correspondence this week, Stanford University's Russ Altman presents an argument against the proposed restructuring at the National Institutes of Health, saying that "it is crucial to separate the engine of discovery from the engine of application." Altman suggests that at the NIH, "there should be separate units to promote discovery, assess outcomes, and engineer the health care system."

And in Nature Communications, an international team led by researchers at Temple University in Philadelphia report their use of molecular manipulation methods to "investigate restriction enzyme reactions with double-stranded DNA oligomers confined in relatively large — and flat — brushy matrices of monolayer patches of controlled, variable density." The team found that as enzymes from the contacting solution can't access dsDNAs from the top-matrix interface, they enter at the matrix sides and "diffuse two-dimensionally in the gap between top- and bottom-matrix interfaces." In its paper, the team discusses the implications of this finding as well as its potential applications.