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

نویسندگان

  • Laura Lagartera
  • Ana González
  • Meike Stelter
  • Pedro García
  • Richard Kahn
  • Margarita Menéndez
  • Juan A Hermoso
چکیده

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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عنوان ژورنال:
  • Acta crystallographica. Section F, Structural biology and crystallization communications

دوره 61 Pt 2  شماره 

صفحات  -

تاریخ انتشار 2005