Overexpression, purification and crystallization of bacteriocin LlpA from Pseudomonas sp. BW11M1.
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.
Parret
Annabel H A
AH
Centre of Microbial and Plant Genetics, Katholieke Universiteit Leuven, 3001 Heverlee, Belgium.
Wyns
Lode
L
De Mot
René
R
Loris
Remy
R
D001430:Bacteriocins / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods; D004926:Escherichia coli / Q000378:metabolism; D008358:Mannose / Q000737:chemistry; D011549:Pseudomonas / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry
D001430:Bacteriocins; D011994:Recombinant Proteins; D008358:Mannose