Publication Abstract from PubMed
Lactococcus lactis is a promising host for (membrane) protein overproduction. Here, we describe a protocol for incorporation of selenomethionine (SeMet) into proteins expressed in L. lactis. Incorporation efficiencies of SeMet in the membrane protein complex OpuA (an ABC transporter) and the soluble protein OppA, both from L. lactis, were monitored by mass spectrometry. Both proteins incorporated SeMet with high efficiencies (>90%), which greatly extends the usefulness of the expression host L. lactis for X-ray crystallography purposes. The crystal structure of ligand-free OppA was determined at 2.4 A resolution by a semiautomatic approach using selenium single-wavelength anomalous diffraction phasing.
Selenomethionine incorporation in proteins expressed in Lactococcus lactis.,Berntsson RP, Alia Oktaviani N, Fusetti F, Thunnissen AM, Poolman B, Slotboom DJ Protein Sci. 2009 May;18(5):1121-7. PMID:19388077[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
