Purification, crystallization and preliminary crystallographic analysis ofthe periplasmic binding protein ProX from Escherichia coli

A periplasmic binding protein (ProX) for the compatible solutes glycine bet aine and proline betaine from Escherichia coli was crystallized using the h anging-drop vapour-diffusion method. Crystals were grown using a protein co ncentration of 10 mg ml(-1) and a precipitant of 26-28% PEG 4000 in 50 mM P IPES pH 6.2-6.4. Native diffraction data to 1.93 Angstrom resolution have b een obtained from crystals at 290 K. The crystals belong to the space group P2(1)2(1)2(1), with unit-cell parameters a = 48.1, b = 55.0, c = 115.7 Ang strom, and contain one molecule per asymmetric unit.