A method for identifying a potential component for the oligosaccharyltransferase -catalysed asparagine-linked ("N-linked") glycosylation selected from the group consisting of (a) a potential oligosaccharide donor, preferably a lipid-linked oligosaccharide or an undecaprenyl pyrophosphate bound oligosaccharide donor, (b) a potential oligosaccharyltransferase, (c) a potential consensus sequence motif polypeptide, and (d) a potential glycosylation inhibitor, comprising the steps of (i) using the atomic coordinates of Table 1, preferably ±2, more preferably ±1.5, most preferably ±1.0 Å root mean square deviation (rmsd) from the backbone atoms, for generating a three-dimensional model of the catalytic domain of the oligosaccharyltransferase of Campylobacter lari, comprising at least three, preferably at least four, more preferably at least six, most preferably all of amino acids D56, R147, D154, D156, E319, R375, Y468, and H485, and/or, preferably and (ii) using the atomic coordinates of Table 1, preferably ±2, more preferably ±1.5, most preferably ±1.0 Å root mean square deviation (rmsd) from the backbone atoms, for generating a three-dimensional model of the polypeptide binding site of the oligosaccharyltransferase of Campylobacter lari, comprising at least two, preferably at least three, more preferably at least four, most preferably all of amino acids M318, R331, W463, W464, D465, and I572, (iii) preferably performing whole body translations and/or rotations on the coordinates of the amino acids of the three-dimensional models of (i) and/or (ii), (iv) using said three-dimensional model(s) of (i), (ii) and/or (iii) for designing or selecting at least one of potential components (a) to (d), (v) providing at least one of said potential components (a) to (d), and (vi) contacting at least one of said potential components (a) to (d) with the further functional components necessary for an oligosaccharyltransferase -catalysed asparagine-linked ("N-linked") glycosylation, (vii) identifying a functional component selected from the group consisting of a functional oligosaccharide donor, preferably a functional lipid-linked oligosaccharide or an undecaprenyl pyrophosphate bound oligosaccharide donor, a functional oligosaccharyltransferase, a functional consensus sequence motif polypeptide, and a functional glycosylation inhibitor. (a) a potential oligosaccharide donor, preferably a lipid-linked oligosaccharide or an undecaprenyl pyrophosphate bound oligosaccharide donor, (b) a potential oligosaccharyltransferase, (c) a potential consensus sequence motif polypeptide, and (d) a potential glycosylation inhibitor, (i) using the atomic coordinates of Table 1, preferably ±2, more preferably ±1.5, most preferably ±1.0 Å root mean square deviation (rmsd) from the backbone atoms, for generating a three-dimensional model of the catalytic domain of the oligosaccharyltransferase of Campylobacter lari, comprising at least three, preferably at least four, more preferably at least six, most preferably all of amino acids D56, R147, D154, D156, E319, R375, Y468, and H485, and/or, preferably and (ii) using the atomic coordinates of Table 1, preferably ±2, more preferably ±1.5, most preferably ±1.0 Å root mean square deviation (rmsd) from the backbone atoms, for generating a three-dimensional model of the polypeptide binding site of the oligosaccharyltransferase of Campylobacter lari, comprising at least two, preferably at least three, more preferably at least four, most preferably all of amino acids M318, R331, W463, W464, D465, and I572, (iii) preferably performing whole body translations and/or rotations on the coordinates of the amino acids of the three-dimensional models of (i) and/or (ii), (iv) using said three-dimensional model(s) of (i), (ii) and/or (iii) for designing or selecting at least one of potential components (a) to (d), (v) providing at least one of said potential components (a) to (d), and (vi) contacting at least one of said potential components (a) to (d) with the further functional components necessary for an oligosaccharyltransferase -catalysed asparagine-linked ("N-linked") glycosylation, (vii) identifying a functional component selected from the group consisting of a functional oligosaccharide donor, preferably a functional lipid-linked oligosaccharide or an undecaprenyl pyrophosphate bound oligosaccharide donor, a functional oligosaccharyltransferase, a functional consensus sequence motif polypeptide, and a functional glycosylation inhibitor. a functional oligosaccharide donor, preferably a functional lipid-linked oligosaccharide or an undecaprenyl pyrophosphate bound oligosaccharide donor, a functional oligosaccharyltransferase, a functional consensus sequence motif polypeptide, and a functional glycosylation inhibitor.