Title | Overexpression, purification and crystallization of bacteriocin LlpA from Pseudomonas sp. BW11M1. |
Publication Type | Journal Article |
Year of Publication | 2004 |
Authors | Parret, A. H. A., L. Wyns, R. De Mot, and R. Loris |
Journal | Acta Crystallogr D Biol Crystallogr |
Volume | 60 |
Issue | Pt 10 |
Pagination | 1922-4 |
Date Published | 2004 Oct |
ISSN | 0907-4449 |
Keywords | Bacteriocins, 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. |
DOI | 10.1107/S0907444904020153 |
Alternate Journal | Acta Crystallogr. D Biol. Crystallogr. |
PubMed ID | 15388953 |
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