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

DOI: 10.1107/S1744309111016770 DOI Help
PMID: 21795789 PMID Help

Authors: Jonathan M. Kirby (University of Bath; Health Protection Agency) , Nethaji Thiyagarajan (University of Bath) , April Roberts (Health Protection Agency) , Clifford Shone (Health Protection Agency) , Ravi Acharya (University of Bath)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 67 (7) , PAGES 762 - 767

State: Published (Approved)
Published: July 2011

Open Access Open Access

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 P21, with unit-cell parameters a = 109.1, b = 61.2, c = 109.2 Å, [beta] = 111.85°, and is estimated to contain two molecules of Cwp19 per asymmetric unit.

Subject Areas: Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

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