Files in this Data Supplement:

• Supplemental file 1 - General description of pectate lyase structures; structure description of the wild type; structural and computational analysis of XcPL mutations with marginal or detrimental effects on thermal stability; CD spectra for Xanthomonas campestris pectate lyase and its variants, A31G, R236F, and A31G/R236F (Fig. S1); top view of wild-type XcPL (Fig. S2); predicted folding free energies vs experimental stabilities of pectate lyase mutants investigated in this study relative to the wild-type protein (Fig. S3); mutagenic oligonucleotide primers (Table S1); success rate for directed evolution (Table S2); crystallographic data collection and refinement (Table S3); energetic contributions to the calculated changes in folding free energy for the most stabilized and destabilized mutants relative to the wild-type pectate lyase (Table S4).
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