We have used single particle cryo electron microscopy to study the binding site of a range of clinically used (and antibiotics in clinical trials) oxazolidones in complex with the ribosome from Staphylococcus aureus to capture a full picture of the range of binding modes that this family of synthetic antibiotics adopt when binding the the ribosome. All of them bind in the peptidyl transferase center of the ribosome, but some such as Radezolid and Tedizolid make a larger range of interations with surrounding rRNA residues. This work has led to a further undertanding to the structure activity relationship of these drugs and has helped explain why these 2nd generation oxazolidinone antibiotics remain unaffected by ribosomal mutations which impart resistance to the first generation drug, linezolid.