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 |
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dc.format |
application/pdf |
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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 |
|