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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt 7):762-7. doi: 10.1107/S1744309111016770. Epub 2011 Jun 30.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / genetics
  • Bacterial Proteins / isolation & purification
  • Cell Wall / chemistry
  • Clostridioides difficile / chemistry*
  • Crystallization
  • Crystallography, X-Ray
  • Gene Expression

Substances

  • Bacterial Proteins