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


Reference:

Kirby, J. M., Thiyagarajan, N., Roberts, A. K., Shone, C. C. and Acharya, K. R., 2011. Expression, purification, crystallization and preliminary crystallographic analysis of a putative Clostridium difficile surface protein Cwp19. Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 67 (7), pp. 762-767.

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Official URL:

http://dx.doi.org/10.1107/s1744309111016770

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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.

Details

Item Type Articles
CreatorsKirby, J. M., Thiyagarajan, N., Roberts, A. K., Shone, C. C. and Acharya, K. R.
DOI10.1107/s1744309111016770
Related URLs
URLURL Type
http://dx.doi.org/10.1107/s1744309111016770Free Full-text
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code25263

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