title: 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, β=111.85°, and is estimated to contain two molecules of Cwp19 per asymmetric unit.
authors.affiliation: Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, England.
authors.forename: Jonathan M
authors.initials: JM
authors.lastname: Kirby
authors.forename: Nethaji
authors.initials: N
authors.lastname: Thiyagarajan
authors.forename: April K
authors.initials: AK
authors.lastname: Roberts
authors.forename: Clifford C
authors.initials: CC
authors.lastname: Shone
authors.forename: K Ravi
authors.initials: KR
authors.lastname: Acharya
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D002473:Cell Wall / Q000737:chemistry; D016360:Clostridioides difficile / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D015870:Gene Expression
chemical_list: D001426:Bacterial Proteins