Overexpression, purification and crystallization of bacteriocin LlpA from Pseudomonas sp. BW11M1.

TitleOverexpression, purification and crystallization of bacteriocin LlpA from Pseudomonas sp. BW11M1.
Publication TypeJournal Article
Year of Publication2004
AuthorsParret, A. H. A., L. Wyns, R. De Mot, and R. Loris
JournalActa Crystallogr D Biol Crystallogr
Volume60
IssuePt 10
Pagination1922-4
Date Published2004 Oct
ISSN0907-4449
KeywordsBacteriocins, Crystallization, Crystallography, X-Ray, Escherichia coli, Mannose, Pseudomonas, Recombinant Proteins
Abstract

LlpA is a bacteriocin produced by Pseudomonas sp. BW11M1 that shows remarkable similarity to a family of mannose-binding plant lectins. A His-tagged version of LlpA was recombinantly produced in Escherichia coli and purified to homogeneity. Single crystals were grown by vapour diffusion and belong to space group P2(1)2(1)2, with unit-cell parameters a = 150.5, b = 154.5, c = 34.2 A. The crystals diffract to at least 2.2 A using synchrotron radiation.
DOI10.1107/S0907444904020153
Alternate JournalActa Crystallogr. D Biol. Crystallogr.
PubMed ID15388953