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Updated: Aug 11, 2026
Production, Crystallization and Structure Determination of C. difficile PPEP-1 via Microseeding and Zinc-SAD
Published on: December 30, 2016
Crystallization and preliminary X-ray diffraction studies of the pneumococcal teichoic acid phosphorylcholine
Laura Lagartera1, Ana González, Meike Stelter
1Departamento de Química-Física de Macromoléculas Biológicas, Instituto Química-Física Rocasolano, CSIC, Serrano 119, 28006 Madrid, Spain.
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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