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

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 P2(1), with unit-cell parameters a=109.1, b=61.2, c=109.2?Å, ?=111.85°, and is estimated to contain two molecules of Cwp19 per asymmetric unit.

SUBMITTER: Kirby JM

PROVIDER: S-EPMC3144791 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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

Kirby Jonathan M JM Thiyagarajan Nethaji N Roberts April K AK Shone Clifford C CC Acharya K Ravi KR

Acta crystallographica. Section F, Structural biology and crystallization communications 20110630 Pt 7

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 P2(1), 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 ...[more]

PMID: 21795789

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