The multiple solvent crystal structures (MSCS) method uses organic solvents as molecular probes to map the binding surfaces of proteins. MSCS was used to map the surface of tailspike protein from Salmonella phage P22 (P22TSP). P22TSP is a viral adhesion protein with receptor binding and destroying functions. P22TSP structures were solved to 1.9 angstroms resolution or better. Crystals of P22TSP were soaked in solvent/aqueous buffer mixtures for data collection with the following organic solvent contents: 50% glycerol; 60% acetone; 60% isopropanol; 50% 2-methyl-2,4 pentanediol; 50% tert-butanol; 50% dimethylsulfoxide; 50% dimethylformamide; 1M trimethylamine-N-oxide; 1M glucose; and neat hexanediol. Structures were solved using the Crystallographic Object�Oriented Toolkit (COOT) and P ython-based H ierarchical EN vironment for I ntegrated X tallography (Phenix) for refinement. The MSCS map depicts hydrophobic pockets not only within P22TSP's known active site, but also at a remote location that constitutes the active site found in evolutionarily related tailspike family members.

Multiple solvent crystal structures of P22TSP

243rd National Meeting (2012)

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