Expression, purification, crystallization and preliminary crystallographic analysis of a putative Clostridium difficile surface protein Cwp19
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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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.
|Creators||Kirby, J. M., Thiyagarajan, N., Roberts, A. K., Shone, C. C. and Acharya, K. R.|
|Departments||Faculty of Science > Biology & Biochemistry|
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