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http://dspace.mediu.edu.my:8181/xmlui/handle/10261/2793| Title: | Crystallization and preliminary X-ray diffraction studies of the pneumococcal teichoic acid phosphorylcholine esterase Pce |
| Keywords: | Choline-binding Proteins Phosphorylcholine Esterases |
| Publisher: | Wiley-Blackwell |
| Description: | 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 Å, β = 112.60°. A 2.7 Å resolution SAD data set from a non-isomorphous Gd-HPDO3A Pce derivative was collected at the gadolinium L III absorption edge using synchrotron radiation. This work was supported by grants from the Spanish Ministry of Science and Technology (BIO2000-1307, BIO2002-02887, BIO2003-01952 and BMC2003-00074). LL holds a fellowship from the Spanish Ministry of Science and Technology. Peer reviewed |
| URI: | http://dspace.mediu.edu.my:8181/xmlui/handle/10261/2793 |
| Other Identifiers: | Acta Crystallogr Sect F Struct Biol Cryst Commun. ; 61(Pt 2): 221–224 (2005 February 1). 1744-3091 http://hdl.handle.net/10261/2793 10.1107/S1744309105001636 |
| Appears in Collections: | Digital Csic |
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