Crystallization and preliminary X-ray diffraction studies of the pneumococcal teichoic acid phosphorylcholine esterase Pce

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Laura LagarteraJuan A Hermoso

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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Citations

Apr 13, 2010·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Inmaculada Pérez-DoradoJuan A Hermoso
Oct 27, 2006·Journal of Molecular Biology·Rubén M BueyJ Fernando Díaz
Jun 11, 2014·Acta Crystallographica. Section D, Biological Crystallography·Meike StelterJuan A Hermoso
May 17, 2005·Nature Structural & Molecular Biology·Juan A HermosoMargarita Menéndez
Nov 2, 2005·Protein Science : a Publication of the Protein Society·Laura LagarteraMargarita Menéndez

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