Expression, purification, crystallization and preliminary crystallographic analysis of a putative Clostridium difficile surface protein Cwp19

Jonathan M. Kirby, Nethaji Thiyagarajan, April Roberts, Clifford Shone, K. Ravi Acharya

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

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 P2 1, 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.

Original languageEnglish
Pages (from-to)762-767
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume67
Issue number7
DOIs
Publication statusPublished - Jul 2011

Keywords

  • Clostridium difficile
  • Cwp19
  • surface proteins

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