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  • Title: Purification, crystallization and preliminary crystallographic analysis of the periplasmic binding protein ProX from Escherichia coli.
    Author: Breed J, Kneip S, Gade J, Welte W, Bremer E.
    Journal: Acta Crystallogr D Biol Crystallogr; 2001 Mar; 57(Pt 3):448-50. PubMed ID: 11223528.
    Abstract:
    A periplasmic binding protein (ProX) for the compatible solutes glycine betaine and proline betaine from Escherichia coli was crystallized using the hanging-drop vapour-diffusion method. Crystals were grown using a protein concentration of 10 mg ml(-1) and a precipitant of 26-28% PEG 4000 in 50 mM PIPES pH 6.2-6.4. Native diffraction data to 1.93 A resolution have been 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 A, and contain one molecule per asymmetric unit.
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