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Crystallization and preliminary X-ray diffraction studies of choline-binding protein F from Streptococcus pneumoniae

AuthorsMolina, Rafael; González, Ana ; Moscoso, Miriam ; García, Pedro ; Stelter, Meike; Kahn, Richard; Hermoso, Juan A.
KeywordsCholine-binding protein F
choline-binding protein F
Issue Date17-Sep-2007
PublisherInternational Union of Crystallography
CitationActa Crystallographica Section F,63(9):742-745(2007)
AbstractCholine-binding protein F (CbpF) is a modular protein that is bound to the pneumococcal cell wall through noncovalent interactions with choline moieties of the bacterial teichoic and lipoteichoic acids. Despite being one of the more abundant proteins on the surface, along with the murein hydrolases LytA, LytB, LytC and Pce, its function is still unknown. CbpF has been crystallized using the hanging-drop vapour-diffusion method at 291 K. Diffraction-quality orthorhombic crystals belong to space group P21212, with unit-cell parameters a = 49.13, b = 114.94, c = 75.69 Å. A SAD data set from a Gd-HPDO3A-derivatized CbpF crystal was collected to 2.1 Å resolution at the gadolinium LIII absorption edge using synchrotron radiation
Description4 páginas, 3 figuras, 1 tabla -- PAGS nros. 742-745
Publisher version (URL)http://dx.doi.org/10.1107/S1744309107035865
Appears in Collections:(CIB) Artículos
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