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

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dc.creator Lagartera, Laura
dc.creator González, Ana
dc.creator Stelter, Meike
dc.creator García, Pedro
dc.creator Kahn, Richard
dc.creator Menéndez, Margarita
dc.creator Hermoso, Juan A.
dc.date 2008-01-30T17:13:53Z
dc.date 2008-01-30T17:13:53Z
dc.date 2005-02-01
dc.date.accessioned 2017-01-31T00:59:53Z
dc.date.available 2017-01-31T00:59:53Z
dc.identifier Acta Crystallogr Sect F Struct Biol Cryst Commun. ; 61(Pt 2): 221–224 (2005 February 1).
dc.identifier 1744-3091
dc.identifier http://hdl.handle.net/10261/2793
dc.identifier 10.1107/S1744309105001636
dc.identifier.uri http://dspace.mediu.edu.my:8181/xmlui/handle/10261/2793
dc.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.
dc.description 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.
dc.description Peer reviewed
dc.format 465908 bytes
dc.format application/pdf
dc.language eng
dc.publisher Wiley-Blackwell
dc.rights openAccess
dc.subject Choline-binding Proteins
dc.subject Phosphorylcholine Esterases
dc.title Crystallization and preliminary X-ray diffraction studies of the pneumococcal teichoic acid phosphorylcholine esterase Pce
dc.type Artículo


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