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

Jonathan M Kirby, Nethaji Thiyagarajan, A K Roberts, C C Shone, K Ravi Acharya

Research output: Contribution to journalArticle

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 angstrom 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 angstrom, beta = 111.85 degrees, 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

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