Ontology highlight
ABSTRACT:
SUBMITTER: Lagartera L
PROVIDER: S-EPMC1952259 | biostudies-literature | 2005 Feb
REPOSITORIES: biostudies-literature
Lagartera Laura L González Ana A Stelter Meike M García Pedro P Kahn Richard R Menéndez Margarita M Hermoso Juan A JA
Acta crystallographica. Section F, Structural biology and crystallization communications 20050201 Pt 2
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-HPDO ...[more]