Large-scale experimental studies show unexpected amino acid effects on protein expression and solubility in vivo in E. coli.

The biochemical and physical factors controlling protein expression level and solubility in vivo remain incompletely characterized. To gain insight into the primary sequence features influencing these outcomes, we performed statistical analyses of results from the high-throughput protein-production pipeline of the Northeast Structural Genomics Consortium. Proteins expressed in E.

In vitro evaluation of right ventricular outflow tract reconstruction with bicuspid valved polytetrafluoroethylene conduit.

Conduits available for right ventricular outflow tract (RVOT) reconstruction eventually become stenotic and/or insufficient due to calcification. In order to reduce the incidence of reoperations we have developed and used a bicuspid valved polytetrafluoroethylene (PTFE) conduit for the RVOT reconstruction. The purpose of this study is to investigate the hemodynamic performance of the new design using a pediatric in vitro right heart mock loop.

Understanding the physical properties that control protein crystallization by analysis of large-scale experimental data.

Crystallization is the most serious bottleneck in high-throughput protein-structure determination by diffraction methods. We have used data mining of the large-scale experimental results of the Northeast Structural Genomics Consortium and experimental folding studies to characterize the biophysical properties that control protein crystallization. This analysis leads to the conclusion that crystallization propensity depends primarily on the prevalence of well-ordered surface epitopes capable of mediating interprotein interactions and is not strongly influenced by overall thermodynamic stability.

Comparisons of NMR spectral quality and success in crystallization demonstrate that NMR and X-ray crystallography are complementary methods for small protein structure determination.

X-ray crystallography and NMR spectroscopy provide the only sources of experimental data from which protein structures can be analyzed at high or even atomic resolution. The degree to which these methods complement each other as sources of structural knowledge is a matter of debate; it is often proposed that small proteins yielding high quality, readily analyzed NMR spectra are a subset of those that readily yield strongly diffracting crystals. We have examined the correlation between NMR spectral quality and success in structure determination by X-ray crystallography for 159 prokaryotic and eukaryotic proteins, prescreened to avoid proteins providing polydisperse and/or aggregated samples.