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  • Title: Crystallization and preliminary X-ray diffraction studies of the pneumococcal teichoic acid phosphorylcholine esterase Pce.
    Author: Lagartera L, González A, Stelter M, García P, Kahn R, Menéndez M, Hermoso JA.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2005 Feb 01; 61(Pt 2):221-4. PubMed ID: 16511000.
    Abstract:
    The pneumococcal phosphorylcholine esterase (Pce or CbpE) is a modular protein that hydrolyses the phosphorylcholine residues present in the teichoic and lipoteichoic acids of the pneumococcal cell wall. Pce has been crystallized using the hanging-drop vapour-diffusion method at 291 K. Diffraction-quality monoclinic crystals belong to space group C2, with unit-cell parameters a = 169.82, b = 57.26, c = 67.44 A, beta = 112.60 degrees. A 2.7 A resolution SAD data set from a non-isomorphous Gd-HPDO3A Pce derivative was collected at the gadolinium L(III) absorption edge using synchrotron radiation.
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