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

Authors :
Kirby, Jonathan M.
Thiyagarajan, Nethaji
Roberts, April K.
Shone, Clifford C.
Acharya, K. Ravi
Source :
Acta Crystallographica: Section F (Wiley-Blackwell). Jul2011, Vol. 67 Issue 7, p762-767. 6p.
Publication Year :
2011

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, β = 111.85°, and is estimated to contain two molecules of Cwp19 per asymmetric unit. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17443091
Volume :
67
Issue :
7
Database :
Academic Search Index
Journal :
Acta Crystallographica: Section F (Wiley-Blackwell)
Publication Type :
Academic Journal
Accession number :
110812794
Full Text :
https://doi.org/10.1107/S1744309111016770