Expression, purification, crystallization and preliminary crystallographic analysis of a putative Clostridium difficile surface protein Cwp19
| Autor: | April K. Roberts, Jonathan M. Kirby, Nethaji Thiyagarajan, K. Ravi Acharya, Clifford C. Shone |
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| Rok vydání: | 2011 |
| Předmět: |
Signal peptide
Biophysics surface proteins Gene Expression Biology Crystallography X-Ray Biochemistry Cwp19 law.invention Bacterial Proteins Structural Biology law Cell Wall Gene expression Genetics Crystallization Clostridioides difficile Resolution (electron density) Space group Clostridium difficile Condensed Matter Physics Crystallography Crystallization Communications Recombinant DNA Monoclinic crystal system |
| Zdroj: | Acta Crystallographica Section F: Structural Biology and Crystallization Communications |
| ISSN: | 1744-3091 |
| Popis: | Cwp19 is a putatively surface-located protein from Clostridium difficile. A recombinant N-terminal protein (residues 27–401) lacking the signal peptide and the C-terminal cell-wall-binding repeats (PFam04122) was crystallized using the sitting-drop vapour-diffusion method and diffracted to 2 Å resolution. Cwp19 is a putatively surface-located protein from Clostridium difficile. A recombinant N-terminal protein (residues 27–401) lacking the signal peptide and the C-terminal cell-wall-binding repeats (PFam04122) was crystallized using the sitting-drop vapour-diffusion method and diffracted to 2 Å resolution. The crystal appeared to belong to the primitive monoclinic space group P21, with unit-cell parameters a = 109.1, b = 61.2, c = 109.2 Å, β = 111.85°, and is estimated to contain two molecules of Cwp19 per asymmetric unit. |
| Databáze: | OpenAIRE |
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