dc.creator | Klinke, Sebastian | |
dc.creator | Otero, Lisandro Horacio | |
dc.creator | Rinaldi, Jimena Julieta | |
dc.creator | Sosa, Santiago | |
dc.creator | Guimarães, Beatriz G. | |
dc.creator | Shepard, William E. | |
dc.creator | Goldbaum, Fernando Alberto | |
dc.creator | Bonomi, Hernan Ruy | |
dc.date.accessioned | 2017-08-28T18:23:07Z | |
dc.date.available | 2017-08-28T18:23:07Z | |
dc.date.created | 2017-08-28T18:23:07Z | |
dc.date.issued | 2014-12 | |
dc.identifier | Klinke, Sebastian; Otero, Lisandro Horacio; Rinaldi, Jimena Julieta; Sosa, Santiago; Guimarães, Beatriz G.; et al.; Crystallization and preliminary X-ray characterization of the full-length bacteriophytochrome from the plant pathogen Xanthomonas campestris pv. campestris; John Wiley & Sons Inc; Acta Crystallographica Section F-structural Biology And Crystallization Communications; 70; 12; 12-2014; 1636-1639 | |
dc.identifier | 1744-3091 | |
dc.identifier | http://hdl.handle.net/11336/23130 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.description.abstract | Phytochromes give rise to the largest photosensor family known to date. However, they are underrepresented in the Protein Data Bank. Plant, cyanobacterial, fungal and bacterial phytochromes share a canonical architecture consisting of an N-terminal photosensory module (PAS2-GAF-PHY domains) and a C-terminal variable output module. The bacterium Xanthomonas campestris pv. campestris, a worldwide agricultural pathogen, codes for a single bacteriophytochrome (XccBphP) that has this canonical architecture, bearing a C-terminal PAS9 domain as the output module. Full-length XccBphP was cloned, expressed and purified to homogeneity by nickel-NTA affinity and size-exclusion chromatography and was then crystallized at room temperature bound to its cofactor biliverdin. A complete native X-ray diffraction data set was collected to a maximum resolution of 3.25 Å. The crystals belonged to space group P43212, with unit-cell parameters a = b = 103.94, c = 344.57 Å and a dimer in the asymmetric unit. Refinement is underway after solving the structure by molecular replacement. | |
dc.language | eng | |
dc.publisher | John Wiley & Sons Inc | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/http://scripts.iucr.org/cgi-bin/paper?S2053230X14023243 | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1107/S2053230X14023243 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/openAccess | |
dc.subject | Xanthomonas Campestris Pv. Campestris | |
dc.subject | Bacteriophytochrome | |
dc.subject | Biliverdin | |
dc.subject | Light-Signalling Pathway | |
dc.subject | Photoreceptor | |
dc.subject | Photosensor | |
dc.title | Crystallization and preliminary X-ray characterization of the full-length bacteriophytochrome from the plant pathogen Xanthomonas campestris pv. campestris | |
dc.type | info:eu-repo/semantics/article | |
dc.type | info:ar-repo/semantics/artículo | |
dc.type | info:eu-repo/semantics/publishedVersion | |