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Figure 5 | Microbial Informatics and Experimentation

Figure 5

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

Figure 5

Biophysical properties of proteins in the different datasets. The distributions of the hydrodynamic statuses of the concentrated protein stock solutions (panel A) and the crystal structure solution rates (panel B) are shown for the Analysis Dataset, the Max ExS Dataset, the 100% Consistent Dataset, and the Human Dataset. Hydrodynamic status was determined as previously described [35]; in brief, a thawed aliquot of the final stock solution from each construct was subject to analytical gel-filtration chromatography monitored by in-line static light-scattering and refractive-index detectors. Non-aggregated samples with less than 85% of the protein in a single hydrodynamic species were classified as polydisperse. Crystal structure solution rate is scored based on PDB deposition via the NESG structure-determination pipeline and does not count constructs yielding diffracting crystals unless they were of sufficient quality to support deposition of the structure. Structure solution rates are shown both as fraction of all targets and as fraction of all constructs.

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