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- Title
Crystallization and preliminary X-ray characterization of the full-length bacteriophytochrome from the plant pathogen Xanthomonas campestris pv. campestris.
- Authors
Klinke, Sebastián; Otero, Lisandro H.; Rinaldi, Jimena; Sosa, Santiago; Guimarães, Beatriz G.; Shepard, William E.; Goldbaum, Fernando A.; Bonomi, Hernán R.
- 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.
- Subjects
CRYSTALLIZATION; PSEUDOMONADACEAE; CATHODE rays; IONIZING radiation; X-ray spectra
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2014, Vol 70, Issue 12, p1636
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X14023243