Please use this identifier to cite or link to this item: http://dspace.mediu.edu.my:8181/xmlui/handle/10261/2793
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dc.creatorLagartera, Laura-
dc.creatorGonzález, Ana-
dc.creatorStelter, Meike-
dc.creatorGarcía, Pedro-
dc.creatorKahn, Richard-
dc.creatorMenéndez, Margarita-
dc.creatorHermoso, Juan A.-
dc.date2008-01-30T17:13:53Z-
dc.date2008-01-30T17:13:53Z-
dc.date2005-02-01-
dc.date.accessioned2017-01-31T00:59:53Z-
dc.date.available2017-01-31T00:59:53Z-
dc.identifierActa Crystallogr Sect F Struct Biol Cryst Commun. ; 61(Pt 2): 221–224 (2005 February 1).-
dc.identifier1744-3091-
dc.identifierhttp://hdl.handle.net/10261/2793-
dc.identifier10.1107/S1744309105001636-
dc.identifier.urihttp://dspace.mediu.edu.my:8181/xmlui/handle/10261/2793-
dc.descriptionThe 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.descriptionThis 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.descriptionPeer reviewed-
dc.format465908 bytes-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherWiley-Blackwell-
dc.rightsopenAccess-
dc.subjectCholine-binding Proteins-
dc.subjectPhosphorylcholine Esterases-
dc.titleCrystallization and preliminary X-ray diffraction studies of the pneumococcal teichoic acid phosphorylcholine esterase Pce-
dc.typeArtículo-
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